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Relevant bibliographies by topics / Post-Translational Protein Processing

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Academic literature on the topic 'Post-Translational Protein Processing'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Post-Translational Protein Processing"

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Johnson, Amy L., Paola Braidotti, Giuseppe G. Pietra, Scott J. Russo, Albert Kabore, Wen-Jing Wang, and Michael F. Beers. "Post-Translational Processing of Surfactant Protein-C Proprotein." American Journal of Respiratory Cell and Molecular Biology 24, no. 3 (March 2001): 253–63. http://dx.doi.org/10.1165/ajrcmb.24.3.4312.

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Zencheck, Wendy D., Hui Xiao, and Louis M. Weiss. "Lysine post-translational modifications and the cytoskeleton." Essays in Biochemistry 52 (May 25, 2012): 135–45. http://dx.doi.org/10.1042/bse0520135.

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PTMs (post-translational modifications) of lysine residues have proven to be major regulators of gene expression, protein–protein interactions, and protein processing and degradation. This is of particular importance in regulating the cytoskeleton, an enormously complex system of proteins responsible for cell motility, intracellular trafficking, and maintenance of cell form and structure. The cytoskeleton is present in all cells, including eukaryotes and prokaryotes, and comprises structures such as flagella, cilia and lamellipodia which play critical roles in intracellular transport and cellular division. Cytoskeletal regulation relies on numerous multi-component assemblies. In this chapter, we focus on the regulation of the cytoskeleton by means of PTMs of lysine residues on the cytoskeletal subunits and their accessory proteins. We specifically address the three main classes of cytoskeletal proteins in eukaryotes that polymerize into filaments, including microfilaments (actin filaments), intermediate filaments and microtubules. We discuss the identification and biological importance of lysine acetylation, a regulator of all three filament types. We also review additional lysine modifications, such as ubiquitination and SUMOylation, and their role in protein regulation and processing.

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Tacchi, Jessica L., Benjamin B. A. Raymond, Paul A. Haynes, Iain J. Berry, Michael Widjaja, Daniel R. Bogema, Lauren K. Woolley, et al. "Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae." Open Biology 6, no. 2 (February 2016): 150210. http://dx.doi.org/10.1098/rsob.150210.

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Mycoplasma hyopneumoniae is a genome-reduced, cell wall-less, bacterial pathogen with a predicted coding capacity of less than 700 proteins and is one of the smallest self-replicating pathogens. The cell surface of M. hyopneumoniae is extensively modified by processing events that target the P97 and P102 adhesin families. Here, we present analyses of the proteome of M. hyopneumoniae- type strain J using protein-centric approaches (one- and two-dimensional GeLC–MS/MS) that enabled us to focus on global processing events in this species. While these approaches only identified 52% of the predicted proteome (347 proteins), our analyses identified 35 surface-associated proteins with widely divergent functions that were targets of unusual endoproteolytic processing events, including cell adhesins, lipoproteins and proteins with canonical functions in the cytosol that moonlight on the cell surface. Affinity chromatography assays that separately used heparin, fibronectin, actin and host epithelial cell surface proteins as bait recovered cleavage products derived from these processed proteins, suggesting these fragments interact directly with the bait proteins and display previously unrecognized adhesive functions. We hypothesize that protein processing is underestimated as a post-translational modification in genome-reduced bacteria and prokaryotes more broadly, and represents an important mechanism for creating cell surface protein diversity.

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O. Solarin, Wen-Jing Wang, Michael, Kolawole. "SYNTHESIS AND POST-TRANSLATIONAL PROCESSING OF SURFACTANT PROTEIN C." Pediatric Pathology & Molecular Medicine 20, no. 6 (November 1, 2001): 471–500. http://dx.doi.org/10.1080/15227950152625792.

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O. Solarin, Wen-Jing Wang, Michael, Kolawole. "SYNTHESIS AND POST-TRANSLATIONAL PROCESSING OF SURFACTANT PROTEIN C." Pediatric Pathology & Molecular Medicine 20, no. 6 (January 2001): 471–500. http://dx.doi.org/10.1080/pdp.20.6.471.500.

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Christensen, Brian, Torben E. Petersen, and Esben S. Sørensen. "Post-translational modification and proteolytic processing of urinary osteopontin." Biochemical Journal 411, no. 1 (March 13, 2008): 53–61. http://dx.doi.org/10.1042/bj20071021.

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OPN (osteopontin) is a highly phosphorylated glycoprotein present in many tissues and body fluids. In urine, OPN is a potent inhibitor of nucleation, growth and aggregation of calcium oxalate crystals, suggesting that it has a role in the prevention of renal stone formation. The role of OPN in nephrolithiasis is, however, somewhat unclear, as it may also be involved in urinary stone formation, and it has been identified among the major protein components of renal calculi. Most likely, the function of OPN in urine is dependent on the highly anionic character of the protein. Besides a very high content of aspartic and glutamic residues, OPN is subjected to significant PTM (post-translational modification), such as phosphorylation, sulfation and glycosylation, which may function as regulatory switches in promotion or inhibition of mineralization. In the present study, we have characterized the PTMs of intact human urinary OPN and N-terminal fragments thereof. MS analysis showed a mass of 37.7 kDa for the intact protein. Enzymatic dephosphorylation and peptide mass analyses demonstrated that the protein contains approximately eight phosphate groups distributed over 30 potential phosphorylation sites. In addition, one sulfated tyrosine and five O-linked glycosylations were identified in OPN, whereas no N-linked glycans were detected. Peptide mapping and immunoblotting using different monoclonal antibodies showed that the N-terminal fragments present in urine are generated by proteolytic cleavage at Arg228–Leu229 and Tyr230–Lys231.

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Verschoor, Ernst J., Ellen G. J. Hulskotte, Joke Ederveen, Marck J. M. Koolen, Marian O. Horzinek, and Peter J. M. Rottier. "Post-translational Processing of the Feline Immunodeficiency Virus Envelope Precursor Protein." Virology 193, no. 1 (March 1993): 433–38. http://dx.doi.org/10.1006/viro.1993.1140.

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Georgopoulou, Niki, Mark McLaughlin, Ian McFarlane, and Kieran C. Breen. "The role of post-translational modification in ϐ-amyloid precursor protein processing." Biochemical Society Symposia 67 (February 1, 2001): 23–36. http://dx.doi.org/10.1042/bss0670023.

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The ϐ-amyloid precursor protein (APP) plays a pivotal role in the early stages of neurodegeneration associated with Alzheimer's disease. An alteration in the processing pattern of the protein results in an increase in the generation of the 40-42-amino-acid ϐ-amyloid (Aϐ) peptide, which coalesces to form insoluble, extracellular amyloid deposits. A greater understanding of the factors that influence APP processing may assist in the design of effective therapeutic agents to halt progression of Alzheimer's disease. APP is a sialoglycoprotein with two potential N-linked glycosylation sites, one of which may contain a complex oligosaccharide chain. An alteration in the glycosylation state of APP by the generation of oligomannosyl oligosaccharides results in a decrease in the secretion of the neuroprotective, soluble form of the protein and a parallel increase in the deposition of the cellular protein within the perinuclear region of the cell. Conversely, the attachment of additional terminal sialic acid residues on to the oligosaccharide chain results in an increase in secretion of soluble APP (sAPPα). One factor that has been widely reported to alter APP processing is the activation of protein kinase C (PKC). This process has been characterized using synaptosomal preparations, which suggests that the PKC action is occurring at the level of the plasma membrane. Furthermore, when cells are transfected with the sialyltransferase enzyme, there is a direct relationship between the sialylation potential of APP and the fold stimulation of sAPPα, after PKC activation. These results suggest that the post-translational modification of APP by glycosylation is a key event in determining the processing of the protein.

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Snijder, Eric J., Johan A. Den Boon, Willy J. M. Spaan, Marianne Weiss, and Marian C. Horzinek. "Primary structure and post-translational processing of the berne virus peplomer protein." Virology 178, no. 2 (October 1990): 355–63. http://dx.doi.org/10.1016/0042-6822(90)90332-l.

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Qin, C., O. Baba, and W. T. Butler. "Post-translational Modifications of SIBLING Proteins and Their Roles in Osteogenesis and Dentinogenesis." Critical Reviews in Oral Biology & Medicine 15, no. 3 (May 2004): 126–36. http://dx.doi.org/10.1177/154411130401500302.

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The extracellular matrix (ECM) of bone and dentin contains several non-collagenous proteins. One category of non-collagenous protein is termed the SIBLING (Small Integrin-Binding LIgand, N-linked Glycoprotein) family, that includes osteopontin (OPN), bone sialoprotein (BSP), dentin matrix protein 1 (DMP1), dentin sialophosphoprotein (DSPP), and matrix extracellular phosphoglycoprotein (MEPE). These polyanionic SIBLING proteins are believed to play key biological roles in the mineralization of bone and dentin. Although the specific mechanisms involved in controlling bone and dentin formation are still unknown, it is clear that some functions of the SIBLING family members are dependent on the nature and extent of post-translational modifications (PTMs), such as phosphorylation, glycosylation, and proteolytic processing, since these PTMs would have significant effects on their structure. OPN and BSP are present in the ECM of bone and dentin as full-length forms, whereas amino acid sequencing indicates that DMP1 and DSPP exist as proteolytically processed fragments that result from scission of X-Asp bonds. We hypothesized that the processing of DMP1 and DSPP is catalyzed by the PHEX enzyme, since this protein, an endopeptidase that is predominantly expressed in bone and tooth, has a strong preference for cleavage at the NH2-terminus of aspartyl residue. We envision that the proteolytic processing of DMP1 and DSPP may be an activation process that plays a significant, crucial role in osteogenesis and dentinogenesis, and that a failure in this processing would cause defective mineralization in bone and dentin, as observed in X-linked hypophosphatemic rickets.

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Dissertations / Theses on the topic "Post-Translational Protein Processing"

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O'Hara, John F. "An investigation of post-translational processing in the transgenic mammary gland." Thesis, University of Kent, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365215.

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Mullins, Fraser Hewitt. "Post-translational processing of microtubule protein during peripheral nerve regeneration." Thesis, University of Liverpool, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.385223.

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Chen, Li. "TAK1-Mediated Post-Translational Modifications Modulate Immune Response: A Dissertation." eScholarship@UMMS, 2005. http://escholarship.umassmed.edu/gsbs_diss/786.

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Innate immunity is the first line of defense against invading pathogens. It provides immediate protection by initiating both cellular and humoral immune reactions in response to a wide range of infections. It is also important to the development of long-lasting and pathogen-specific adaptive immunity. Thus, studying of the innate immunity, especially the pathogen recognition and signaling modulation, is crucial for understanding the intrinsic mechanisms underlying the host defense, as well as contributing the development of the fight against infectious diseases. Drosophila is an ideal model organism for study of innate immunity. Comparing to mammals, Drosophila immunity is relative conserved and less redundant. A variety of molecular and genetic tools available add further convenience to the research in this system. My work is focused on the signaling modulation by post-translational modification after activation. In these studies I demonstrated in the center of Imd pathway, the Imd protein undergoes proteolytic cleavage, K63-polyubiquitination, phosphorylation, K63-deubiquitination and K48-polyubiquitination/degradation in a stimulation-dependent manner. These modifications of Imd play a crucial role in regulating signaling in response to infection. The characterization of ubiquitin-editing event provides a new insight into the molecular mechanisms underlying the activation and termination of insect immune signaling pathway.

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Chen, Li. "TAK1-Mediated Post-Translational Modifications Modulate Immune Response: A Dissertation." eScholarship@UMMS, 2015. https://escholarship.umassmed.edu/gsbs_diss/786.

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Innate immunity is the first line of defense against invading pathogens. It provides immediate protection by initiating both cellular and humoral immune reactions in response to a wide range of infections. It is also important to the development of long-lasting and pathogen-specific adaptive immunity. Thus, studying of the innate immunity, especially the pathogen recognition and signaling modulation, is crucial for understanding the intrinsic mechanisms underlying the host defense, as well as contributing the development of the fight against infectious diseases. Drosophila is an ideal model organism for study of innate immunity. Comparing to mammals, Drosophila immunity is relative conserved and less redundant. A variety of molecular and genetic tools available add further convenience to the research in this system. My work is focused on the signaling modulation by post-translational modification after activation. In these studies I demonstrated in the center of Imd pathway, the Imd protein undergoes proteolytic cleavage, K63-polyubiquitination, phosphorylation, K63-deubiquitination and K48-polyubiquitination/degradation in a stimulation-dependent manner. These modifications of Imd play a crucial role in regulating signaling in response to infection. The characterization of ubiquitin-editing event provides a new insight into the molecular mechanisms underlying the activation and termination of insect immune signaling pathway.

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Scholz, Claus Jürgen. "Analyse der Expression und posttranslationalen Modifikation des Tetraspanins Tspan-1 in Ovarialkarzinomzellen." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:289-vts-59801.

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Chiocco, Matthew J. "Beta-secretase transgenic mice effects of BACE1 and BACE2 on Alzheimer's disease pathogenesis /." Connect to text online, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=case1111597750.

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Li, M. "In vitro reconstitution of the extraordinary post-translational processing of Concanavalin A precursor : circular sequence permutation by enzymatic cleavages and protein splicing." Thesis, Swansea University, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.637901.

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The lectin Concanavalin A is processed in planta by a splicing-mediated circular permutation of its initial single-chain precursor, pro-Concanavalin A. Active (carbohydrate-binding) protein conformations can be purified by dextran-affinity chromatography. This thesis demonstrates in vitro splicing by asparaginyl endopeptidase of two cofolded polypeptide fragments (A- and B-chains) corresponding to Concanavalin A precursors. This ligation of A- and B-chains was enzyme-, temperature- and pH-dependent. The 9-residue extension at the C-terminus of A-chain is essential for splicing. To test whether correct cofolding and an intervening spacer are required for maturation, recombinant A- and B-chains without spacer sequence were purified and refolded separately. Asparaginyl endopeptidase was again absolutely required for ligation of non-cofolded A- and B-chains. Correct folding is crucial to form an active structure, but is less important for enzyme-mediated splicing. Protein splicing of two-chain forms of precursors was clearly evident from the large decrease in electrophoretic mobility of ligated product. However, interpretation of proteolytic cleavage patterns was difficult. In vivo maturation could be reconstituted in vitro using recombinant pro-Concanavalin A (single-chain, active) with asparaginyl endopeptidase. Enzyme could also splice synthetic peptides corresponding to processing-sequences of precursor proteins. Two short peptides were ligated to form a new longer peptide as indicated by reverse-phase chromatography. It was generally observed that increasing the pH from 5 to 7.5 changed the balance away from proteolytic cleavages (hydrolysis) and towards protein (or peptide) ligation (aminolysis). Promotion of splicing at higher pH indicates that availability of the unprotected (nucleophilic) form of the attacking terminal a-amino group is a major factor in determining product formation. Other factors (substrate conformation, concentrations, temperature and incubation time) may also influence the outcome.

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King, Henry Owain. "Role of ApoEr2 isoforms in the cellular processing of the Alzheimer's amyloid precursor protein : insights into the post translational processing of ApoEr2 and identification of a novel mechanism of APP regulation." Thesis, University of Leeds, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.574497.

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Alzheimer's disease (AD) is a debilitating neurodegenerative disease that affects millions of people worldwide. AD is characterised by the accumulation aggregation and deposition within the brain of amyloid ~ (A~), a 40-42 residue peptide, and hyperphosphorylated Tau. A~ is a cleavage product of the amyloid precursor protein (APP) produced by the sequential cleavage of the ~-secretase, 8ACE1 (~-sjte APP Cleaving enzyme), and the v-secretase. APP can also be proteolytically processed by an alternative pathway where an a-secretase cleaves APP within the A~ region followed by v-cleavage. This precludes the formation of A~. Protein-protein interactions play an important role in regulating protein function; elucidating how the interactions between APP and other proteins affect A~ accumulation in an age-dependent manner is crucial to understanding AD progression. The Apolipoprotein E receptor 2 (ApoEr2) interacts with APP and alters its cleavage, though its exact effect is unclear as it has been shown to both increase and decrease ~-secretase cleavage of APP. To understand the reason for this disparity, 3 different splice variants of ApoEr2 have been expressed in HEK cells and their effects on the levels of APP cleavage products assessed. The isoforms chosen were a full length form (ApoEr2 FL), a form lacking the exon 5 and 15 encoded regions (ApoEr2 1:::.5,15), and a form lacking exon 18 (ApoEr2 1118) which encodes a cytoplasmic proline rich domain. These were chosen as all 3 isoforrns are brain expressed and have been used by different groups in investigating the effects of ApoEr2 on APP processing. It was found that 2 isoforms of ApoEr2 (ApoEr2 FL and 1:::.5,15) caused a reduction in ~- and a-cleavage of APP of -50%, where as ApoEr2 l::.18 increased ~-cleavage -200% whilst having no effect on a- cleavage, To identify the mechanism behind the variation between the isoforms effect on APP Cleavage, the post translational processing of ApoEr2 has been investigated, ApoEr2 was identified as being both N- and O-glycosylated and differences between the isoforms of ApoEr2 in the extent of fully glycosylatyed protein were identified. ApoEr2 l::.5,15 was produced as a fully glycosylated protein. With ApoEr2 FL and 1118 a partially glycosylated protein is also detectable at -25% of total ApoEr2 1:.18 and 40% of total ApoEr2 FL ApoEr2 is also shed from the plasma membrane and there were differences in the shedding of the isoforms of ApoEr2, with ApoEr2 1:.5,15 shed to a lower level than ApoEr2 FL or 1:::.18. The enzyme responsible for the shedding of ApoEr2 has been identified as ADAM10, an enzyme also involved in cleaving APP. The subcellular localisation of ApoEr2 was also investigated and increased detection of ApoEr2 in the early endosome may explain the isoform specific effect of ApoEr2 on APP cleavage. This work has shown for the first time that different splice forms of ApoEr2 have radically different effects on APP proteolytic processing, The fact that splice forms of a protein can have such different effects on APP processing shows that the regulation of APP cleavage is exceedingly complex. This work has also significantly extended what is known about the post translational processing of ApoEr2 with the identification of the enzyme responsible for the shedding of ApoEr2 and has shown that there is substantial variation in post translational processing of the different isoforms of ApoEr2.

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Turunen, S. (Sanna). "Protein-bound citrulline and homocitrulline in rheumatoid arthritis:confounding features arising from structural homology." Doctoral thesis, Oulun yliopisto, 2014. http://urn.fi/urn:isbn:9789526203904.

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Abstract Rheumatoid arthritis (RA) is an autoimmune disease causing inflammation of synovial joints, which may lead to permanent changes in cartilage and bone tissues. RA patients have antibodies binding to citrullinated and also to carbamylated proteins. Antibodies binding to citrulline are associated with more severe disease progression and may already appear years before clinical disease onset. Citrulline and the lysine carbamylation product, homocitrulline, are similar in structure. Citrullinated proteins have been studied in RA and in neurological diseases, but researchers have been unaware of the effect of homocitrulline in citrulline detection methods. The purpose of the present study was to clarify the features of protein-bound citrulline and homocitrulline in relation to research done on citrullination and in immunological reactions related to rheumatoid arthritis. In the first study of this thesis the confounding role of homocitrulline in citrulline detection was shown. In the first and second study the features of experimentally induced antibodies were assessed. The antibodies induced with citrulline- and homocitrulline-containing protein structures were shown to react both with the ureido groups and the protein structures. The antibodies were able to distinguish between citrulline and homocitrulline in the same sequence even though binding to both. In the third study the simultaneous presence of citrulline and homocitrulline in RA synovial tissue was shown. In conclusion, considering the simultaneous presence of citrulline and homocitrulline and the binding features of the experimentally induced antibodies, homocitrulline could have a yet unsolved role in RA. Secondly, the existence of homocitrulline should be borne in mind in studies on citrullination
Tiivistelmä Nivelreuma on niveltulehduksen aiheuttava autoimmuunitauti, joka voi johtaa pysyviin muutoksiin nivelen rusto- ja luukudoksessa. Nivelreumaa sairastavilla esiintyy vasta-aineita sitrullinoituneita ja karbamyloituneita proteiineja vastaan. Sitrulliiniin sitoutuvia vasta-aineita voi esiintyä elimistössä jo vuosia ennen taudin puhkeamista, ja niiden esiintyminen on yhdistetty vaikeampaan taudinkuvaan. Sitrulliini ja lysiinin karbamylaatiotuote homositrulliini ovat rakenteellisesti samankaltaisia. Proteiinien sitrullinaatiota on tutkittu nivelreumassa ja neurologisissa taudeissa, mutta homositrulliinin olemassaoloa tai sen vaikutusta tutkimusmenetelmiin ei ole huomioitu. Tämän tutkimuksen tarkoituksena oli selvittää proteiineihin sitoutuneiden sitrulliinin ja homositrulliinin ominaisuuksia aikaisempiin tutkimuksiin ja nivelreuman immunologisiin reaktioihin liittyen. Tässä tutkimuksessa homositrulliinin osoitettiin häiritsevän sitrulliinin tunnistamista. Ensimmäisessä ja toisessa osatyössä aiheutettiin kokeellisesti vasta-aineita sitrulliinia ja homositrulliinia sisältävillä proteiinirakenteilla. Vasta-aineiden havaittiin reagoivan sekä ureidoryhmän että proteiinirakenteen kanssa. Vasta-aineet pystyivät erottamaan sitrulliinin ja homositrulliinin toisistaan samassa rakenteessa, vaikka sitoutuivat kumpaankin. Kolmannessa osatyössä osoitettiin, että sitrulliinia ja homositrulliinia esiintyy samanaikaisesti nivelreumapotilaan tulehtuneessa nivelkalvossa. Tutkimus osoitti, että sitrulliinin ja homositrulliinin samanaikainen esiintyminen ja kokeellisesti aiheutettujen vasta-aineiden ominaisuudet huomioiden homositrulliinilla voi olla jokin toistaiseksi selvittämätön rooli nivelreumassa. Homositrulliinin olemassaolo on syytä huomioida sitrullinaatiota tutkittaessa

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Cruz, Tapias Paola. "Un mécanisme de trans-méthylation entre les deux principales méthyltransférases de H3K9 SETDB1 et SUV39H1, régule l'établissement de l'hétérochromatine." Thesis, Sorbonne Paris Cité, 2018. http://www.theses.fr/2018USPCC285.

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La méthylation de la lysine 9 de l’histone 3 (H3K9), établie par les lysine méthyltransférases (KMTs) SETDB1, SUV39H1, G9A et GLP, représente un mécanisme épigénétique central dans la régulation du destin cellulaire. En particulier, la methylation d’H3K9 est directement impliquée dans la formation de l’hétérochromatine et l’extinction des gènes. Notre laboratoire a montré que les principales KMTs (SETDB1, G9A, GLP et SUV39H1) spécifiques de H3K9 forment un méga-complexe impliqué dans la répression transcriptionnelle, probablement via une coopération pour établir les différents niveaux de méthylation. Néanmoins, la régulation des complexes de H3K9 KMT n’est jusqu’à présent pas bien comprise. Il est à noter que des modifications post-traductionnelles (PTM) ont été impliquées dans la régulation des fonctions des KMTs. Dans ce contexte, mon projet visait à comprendre comment la méthylation de SETDB1 régulerait son activité (incorporation dans des complexes, interaction avec ses partenaires, recrutement à la chromatine). Le but étant d’établir quel impact auraient ces modifications de SETDB1 sur la formation de l’hétérochromatine, l’expression des gènes et la régulation du destin cellulaire. SETDB1 est cruciale lors du développement et de la différençiation cellulaire. De plus, SETDB1 est essentielle pour la pluripotence et le renouvellement des cellules souches embryonnaires murines (mESC). L’inactivation génique de ou KO de Setdb1 est létal au stade préimplantatoire à 7,5 jours post-coïtum (dpc). En plus des histones, SETDB1 méthyle d’autres protéines comme UBF, ING2 et p53. Mes résultats montrent notamment, que SETDB1 s’autométhyle sur les lysines K1170 et K1178 localisées dans le domaine catalytique SET. SETDB1 et SUV39H1 coordonnent l’établissement et la maintenance de H3K9me3 dans l’hétérochromatine péricentromérique constitutive et co-régulent de nombreuses cibles génomiques dans l’hétérochromatine, dont les éléments transposables comme les Long Interspersed Nuclear Elements (LINEs) et les rétrovirus endogènes (ERVs). Comme SUV39H1 est une triméthyltransférase qui utilise H3K9me1 ou H3K9me2 comme substrat primaire, SETDB1 pourrait probablement fournir les mono- ou di-méthyl H3K9. Mes résultats suggèrent un modèle dans lequel l’auto-méthylation de SETDB1 est pré-requise à la trans-méthylation subséquente par SUV39H1. Ce mécanisme pourrait réguler non seulement l’interaction physique entre SETDB1 et SUV39H1, via le chromodomaine de SUV39H1, mais aussi leur coopération dans l’établissement et la maintenance des blocs (grands domaines) d’hétérochromatine et l’extinction des éléments transposables, au moins dans les cellules souches. Ainsi, nous souhaitons mieux comprendre comment le « dialogue » entre ces deux H3K9 KMT majeures, SETDB1 et SUV39H1, est impliqué dans leurs interactions et leurs recrutements aux loci cibles
Histone H3 lysine 9 (H3K9) methylation, which is established by the lysine methyltransferases (KMTs) SETDB1, SUV39H1, G9A and GLP, is a central epigenetic mechanism involved in cell fate regulation. In particular, H3K9 methylation is directly involved in heterochromatin formation and gene silencing. Our lab showed that the main H3K9 KMTs (SETDB1, G9A, GLP and SUV39H1) form a functional megacomplex involved in transcriptional silencing, probably via the cooperative establishment of the different H3K9 methylation levels. However, up to now, the regulation of the H3K9 KMT complexes is not fully understood. Interestingly, post-translational modifications (PTMs) have been implicated in the regulation of H3K9 KMT functions. In this, my PhD thesis aimed to decipher how methylation of SETDB1, regulates its activity (complex formation, interaction with partners, recruitment to chromatin), which ultimately could impact on heterochromatin formation, gene expression and cell fate regulation. SETDB1 is crucial during development and cellular differentiation. Moreover, SETDB1 is essential in mouse embryonic stem cells (mESCs) pluripotency and self-renewal, Setbd1 KO is lethal at the peri-implantation stage at 7.5 days postcoitum (dpc). Beside histones, SETDB1 is also able to methylate other proteins (e.g. UBF, ING2, p53). Notably, my current data show that SETDB1 undergoes (auto)methylation on the lysines K1170 and K1178 located inside its catalytic SET domain. SETDB1 and SUV39H1 coordinate the establishment and maintenance of H3K9me3 at constitutive pericentromeric heterochromatin and co-regulate many genomic targets within heterochromatin, including transposable elements, such as long interspersed nuclear elements (LINEs) and endogenous retroviruses (ERVs). Since SUV39H1 is a H3K9 tri-methyltransferase that uses H3K9me1 or H3K9me2 as a primary substrate, SETDB1 could probably provide mono- or di-methylated H3K9. Interestingly, my results point to a model in which SETDB1 auto-methylation paves the path to a subsequent trans-methylation by SUV39H1. This mechanism could regulate not only the SETDB1/SUV39H1 physical interaction (via the SUV39H1 chromodomain), but also cooperation in the establishment and maintenance of both heterochromatin blocks (large domains) and transposable elements (TEs) silencing, at least in ES cells. Thus, we would like to better understand how the crosstalk between these two key H3K9 KMTs, SETDB1 and SUV39H1, occurs in terms of interaction and recruitment to target loci

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Books on the topic "Post-Translational Protein Processing"

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Walsh, Gary. Post-translational modification of protein biopharmaceuticals. Weinheim: Wiley-VCH, 2009.

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Posttranslational modification of proteins: Expanding nature's inventory. Englewood, Colo: Roberts and Co. Publishers, 2006.

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NATO Advanced Study Institute on Cellular Regulation by Protein Phosphorylation (1990 La Londe les Maures, France). Cellular regulation by protein phosphorylation. Berlin: Springer-Verlag, 1991.

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1959-, Martin Bruce L., and Wang Jerry H, eds. Co- and post-translational modification of proteins: Chemical principles and biological effects. New York: Oxford University Press, 1994.

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Animal cell biotechnology: In biologics production. Berlin: De Gruyter, 2015.

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D, Hames B., and Higgins S. J, eds. Post-translational processing: A practical approach. Oxford: Oxford University Press, 1999.

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Walsh, Christopher. Posttranslational Modification of Proteins: Expanding Nature's Inventory. Roberts and Co. Publishers, 2005.

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(Editor), S. J. Higgins, and B. D. Hames (Editor), eds. Post-Translational Processing: A Practical Approach (The Practical Approach Series, 203). Oxford University Press, USA, 1999.

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Post-Translational Processing: A Practical Approach (The Practical Approach Series, 203). Oxford University Press, USA, 1999.

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Sutovsky, Peter. Posttranslational Protein Modifications in the Reproductive System. Springer, 2016.

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Book chapters on the topic "Post-Translational Protein Processing"

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Morris, Howard R., Anne Dell, Maria Panico, Roy McDowell, and Ashraf Chatterjee. "Analysis of Post-translational Modification and Processing by High Mass FAB Mass Spectrometry." In Methods in Protein Sequence Analysis, 206–18. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73834-0_28.

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Gorman, Jeffrey J., Gary L. Corino, and Stephen J. Mitchell. "A Fluorescent Labelling Procedure to Facilitate Protein Isolation for Rapid Structural Analysis on a Microscale: Application to Analysis of Post-translational Processing of Newcastle Disease Virus Proteins." In Methods in Protein Sequence Analysis, 302–9. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73834-0_40.

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Katunuma, Nobuhiko, Masae Takahashi, and Tadashi Tezuka. "Post-translational Proteolytic Processing on Intracellular Proteins by Cathepsins and Cystatins." In Post-Translational Modifications in Health and Disease, 425–56. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6382-6_18.

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Ailor, E., and M. J. Betenbaugh. "Engineering Post-Translational Processing of Recombinant Proteins Produced in Insect Cell Culture." In Cell Engineering, 29–42. Dordrecht: Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-011-4315-8_2.

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Buxbaum, Joseph D. "Post-translational control of the amyloid β-protein precursor processing." In Pathobiology of Alzheimer's Disease, 99–114. Elsevier, 1995. http://dx.doi.org/10.1016/b978-012286965-5/50008-x.

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Wu, Zhenxing, Xiaofen Mo, Chengbo Lang, and Jinjing Luo. "The Function of FEN1 is Regulated by Post-Translational Modification." In Post-Translational Modifications in Cellular Functions and Diseases [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96635.

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Flap endonuclease 1 (FEN1) is a multifunctional DNA branching nuclease. Post-translational modifications (PTMs) exist in this protein widely, including phosphorylation, methylation, acetylation, ubiquitination and small ubiquitination modification (SUMO). Here, we make a summary for those PTMs studies on FEN1, to illustrate relationships between mutations of those amino acids and their functions alteration of FEN1. Numerous evidences have confirmed that dysfunction of FEN1 would lead to genome instability, and then induce a variety of chromosome-related diseases ultimately, including tumors. On one hand, interaction partner also stimulates FEN1 nuclease activity, to further ensure an effective role in the processing of different DNA structures; on the other hand, PTMs may regulate protein-protein interactions and FEN1’s cellular localization.

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Conference papers on the topic "Post-Translational Protein Processing"

1

Kotorashvili, A., S. Mulugeta, S. Guttentag, and MF Beers. "Pepsinogen C Is a Candidate Protease for Post-Translational Processing of Surfactant Protein C." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a6265.

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Jorgensen, M. J., MJ Rabiet, A. B. Cantor, B. Furie, C. L. Brown, C. B. Shoemaker, and B. C. Furie. "VITAMIN K-DEPENDENT γ-CARBOXYLATION OF FACTOR IX REQUIRES A RECOGNITION SITE CONTAINED WITHIN THE PROPEPTIDE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643564.

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The vitamin K-dependent proteins, including Factor IX (FIX), are calcium-binding proteins that undergo vitamin K-dependent post-translational modification to convert amino terminal glutamic aoid residues to Gla residues. Sequence homology among the propeptides of these proteins suggests a role for this region in designating the adjacent glutamic acid-rich domain for γ-carboxylation during intraoellular processing. Mutations vere made in the propeptide (residues -1 to -18) of FIX, and the effects on γ-carboxylation were assessed. The human FIX cDNA coding sequenoe was modified using oligonucleotide-directed site-specific mutagenesis and was expressed in Chinese hamster ovary cells. The extent of γ-carboxylation of secreted FIX was determined by (1) ability to interact with conformation-specific antibodies directed against the Gla-dependent, metal-stabilized, native structure of FIX, and (2) direct Gla analysis of the alkaline hydrolysate. Using the unmodified coding sequence, 64 ± 17 % of recombinant Factor IX bound to the conformation-specific antibodies, and 9.4 ± 0.7 Gla residues were found (compared with 12 Gla in plasma FIX). When the 18-residue propeptide was deleted, secreted FIX contained no detectable native FIX antigen and no detectable Gla. Similarly, point mutations leading to substitution of Ala for Phe at residue -16 or Glu for Ala at residue -10 led to secretion of FIX containing 2% and 6% native antigen, respectively, and approximately 1-2 Gla residues. The molecular weight of each of the reoombinant FIX species, as estimated by SDS-PAGE, was identical to that of plasma FIX. NH2-terminal sequence analysis of the mutant FIX speoies yielded the NH2-terminal sequence of plasma FIX. These data indicate that the mutations made in the propeptide did not interfere with intracellular proteolytic prooessing of FIX. We conolude that the FIX propeptide participates in defining a recognition site that designates an adjacent glutamic acid-rich domain for γ-carboxylation. The association of the propeptide with the γ-carboxylation recognition site provides the first demonstration of a specific function served by a propeptide in post-translational protein processing.

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Polack, B., A. Duperray, and R. Berthier. "PLATELET AND ENDOTHELIAL CELL CYTOADHESINS ARE BIOSYNTHESIZED AND PROCESSED VIA SIMILAR PATHWAYS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642815.

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The cytoadhesin family represents a group of heterodimeric adhesion receptors with common structural, fonctional and immunochemical properties. Platelet and endothelial cell (EC) GPIIbIII a related proteins exemplify two members of this family. In the present study the biosynthesis and processing of EC GPIIbIII a were examined and compared with that of platelet GPIIbIIIa to verify whether the diversity of these cytoadhesins was related to post translational events.Endothelial cells of human umbilical cord vein origin were metabolicaly labeled with 35S-methionine. The newly synthesized proteins were analyzed and immunoprecipitated with polyclonal antibodies against the purified platelet GPIIbllla complex and the isolated GPIIb and GPIIIa. Under non-reducing conditions three bands were detected at 135 kD, 125 kD and 90kD with the anti GPIIbIIIa. Samples obtained from pulse chase experiments and analysed under non reducing conditions indicated that the 135 kD band derived from the 125 kD band. Under reducing conditions the 135 kD generated two bands at 118 kD and 25 kD. The 125 KD band also gave a 118 kD band and the 90 kD band shifted to 100 kD. These results indicated that the mature form of 135 kD is composed of two polypeptidic chains which derive from a common single chain precursor similar to that observed in the megakaryocyte. The mature protein and the precursor molecule were not recognised by anti GPIIb antibodies. Also immunoprecipitated by polyclonal anti GPIIIa antibodies was a single chain protein of 100kD. In addition, endoglycosidase treatement showed that both EC GPIIIa and platelet GPIIIa were glycosylated protein of the high mannose type.These results indicate that although structural differences exists between platelet and endothelial cell GPIIbllla, the two membrane glycoproteins have a similar cellular transit.

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Verweij, C. L., R. Quadt, E. Briët, and H. Pannekoek. "TWO VON WILLEBRAND FACTOR (vWF) GENE POLYMORPHISMS SEGREGATE WITH VON WILLEBRAND'S DISEASE (vWD) TYPE IIA: ASSIGNMENT OF THE DEFECTIVE GENE LOCUS IN vWD TYPE IIA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644646.

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Patients with autosomal, dominant von Willebrand's disease (vWD) type IIA display a decreasedristocetin cofactor activity and lack the large and intermediate size von Willebrand factor (vWF) multimers. As yet the cause for this abnormal vWF protein is not known. In this study we determined whether vWD type IIA is due to a mutation in the vWF gene or by a defect in another gene involved, in for example, vWF processing.Restriction fragment-length polymorphisms (RFLP's), using the enzymes BgIII and XbaI in conjunction with human vWF cDNA probes, have been described. Restriction endonuclease analysis of genomic vWF DNA revealed that these genetic marker are located within the vWF gene. The vWF gene was determined to comprise about 160 kb and harbors at least 20 exons. The RFLP's were applied to study the segregation of alleles associated withvWD type IIA in a comprehensive, affected family. It is demonstrated that both RFLP's are completely linked with the vWD type-IIA trait. From this finding, we conclude that the defect, causing the vWD type IIA, is most likely due to a mutation in the vWF gene and not to a mutation in another gene involved in, for example, post-translational processing of the vWF protein.

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Marquerie, G., A. Duperray, G. Uzan, and R. Berthier. "BIOSYNTHETIC PATHWAYS OF THE PLATELET FIBRINOGEN RECEPTOR IN HUMAN MEGAKARYOCYTES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642954.

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Interaction between cells and between cells and extracellular matrices are critical for a number of biological processes, including organ development, cell differenciation, cell motility, and the inimune' response. These interactions are mediated by a family of adhesion receptors that recognize short sequences such as Arg-Gly-Asp (RGD). These receptors share similar structural properties. They are heterodimers composed of a and B subunits and sometime express common epitopes. This suggests that the structural and functional relationship of these receptors may result from the transcription of related genes or may arise from cell specific post-transcriptional events. Thus, analysis of the biosynthesis and processing of these receptors would provide valuable insights into the molecular mechanism which control their expression at the surface,of different cells. Platelet membrane glycoprotein (GP) IIb-IIIa is a member of this receptor family. This protein is a non covalent heterodimer composed of two distinct polypeptides, Glib which consists of two subunits Ilba and IlbB (Mr = 116 kD, Mr = 25 kD) and GPIIIa (Mr = 100 kD, reduced). GPIIb-IIIa functions at site of platelet aggregation and serves as receptor for RGD containing factors including fibrinogen, fibronectin and von Willebrand factor. We report here on the investigation of the biosynthetic pathways of this RGD receptor in human megakaryocytes. High number of megakaryocytic cells from the megakaryoblastic stage to the polyploid mature megakaryocyte were obtained from liquid culture of cryopreserved leukocyte stem cell concentrates from patients with chronic myelogenous leukemia (CML). After sorting, using a FACS IV and indirect immunofluores-cent labeling with monoclonal antibodies anti-GPIIb-IIIa, 95 % of the cells in culture were of the megakaryocytic lineage. These megakarocytes represented an excellent tool to delineate at the molecular level events associated with the biosynthesis of GPIIb-IIIa.Metabolic labeling and pulse-chase experiments indicated that GPIIb and GPIIIa are synthesized from separate mRNA and that the two subunits of GPIIb derive from a common precursor. This was further confirmed by cell-free translation of megakaryocyte mRNA and the identification of separate cDNA containing sequences coding for the pro-GPIIb and for GPIIIa. These cDNA were isolated from a Xgt11 expression library constructed with purified megakaryocyte RNA, and were used to size the messengers coding for the two polypeptides. A single mRNA species of 3.9 kB was found to encode the pro-GPIIb, whereas two different mRNA species of 2.9 kB and 4. 1 kB were identified with the GPIIIa cDNA.The newly synthesized GPIIIa associates early with the pro-GPIIb in the rough endoplasmic reticulum. Examination of the glycosylation pathways with endoglycosidase H, tunicamycin and monensin indicated that high mannose oligosaccharides are added to the GPIIIa and pro-GPIIb polypeptide backbone. The pro-GPIIb is then processed with conversion of high mannose to the complex type carbohydrate, whereas GPIIIa remains endoH sensitive. Glycosylation of pro-GPIIb-IIIa and processing of oligosaccharides are prerequisite for proteolytic maturation of pro-GPIIb and the expression of the mature complex at the surface of the cell. Thus post-translational processing of GPIIb-IIIa requires an early assembly of the complex. This may have important implications in the maturation of megakaryocyte granules and in the molecular mechanism underlying the Glanzmann thrombastenic disease.

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