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Journal articles on the topic 'Proteine serine'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Maroncle, Nathalie M., Kelsey E. Sivick, Rebecca Brady, Faye-Ellen Stokes, and Harry L. T. Mobley. "Protease Activity, Secretion, Cell Entry, Cytotoxicity, and Cellular Targets of Secreted Autotransporter Toxin of Uropathogenic Escherichia coli." Infection and Immunity 74, no. 11 (2006): 6124–34. http://dx.doi.org/10.1128/iai.01086-06.

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ABSTRACT The secreted autotransporter toxin (Sat), found predominantly in uropathogenic Escherichia coli, is a member of the SPATE (serine protease autotransporters of Enterobacteriaceae) family and, as such, has serine protease activity and causes cytopathic effects on various cell types. To assess the contribution of the serine protease active site to the mechanism of action of Sat, mutations were made in the first (S256I), in the second (S258A), or in both (S256I/S258A) serine residues within the active site motif. Mutations in the first or both serines reduced protease activity to backgrou

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Barrasa, M. Inmaculada, Noam Y. Harel, and James C. Alwine. "The Phosphorylation Status of the Serine-Rich Region of the Human Cytomegalovirus 86-Kilodalton Major Immediate-Early Protein IE2/IEP86 Affects Temporal Viral Gene Expression." Journal of Virology 79, no. 3 (2005): 1428–37. http://dx.doi.org/10.1128/jvi.79.3.1428-1437.2005.

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ABSTRACT The 86-kDa major immediate-early protein (IE2/IEP86) of human cytomegalovirus (HCMV) contains a serine-rich region (amino acids 258 to 275) with several consensus casein kinase II (CKII) sites. We performed extensive mutational analysis of this region, changing serines to alternating alanines and glycines. Mutation of the serines between amino acids 266 and 275 eliminated in vitro phosphorylation by CKII. In vitro CKII phosphorylation of the serines between amino acids 266 and 269 or between amino acids 271 and 275 inhibited the ability of IE2/IEP86 to bind to TATA-binding protein. Co

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3

Calvo, E., D. Escors, J. A. López, et al. "Phosphorylation and subcellular localization of transmissible gastroenteritis virus nucleocapsid protein in infected cells." Journal of General Virology 86, no. 8 (2005): 2255–67. http://dx.doi.org/10.1099/vir.0.80975-0.

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The nucleocapsid (N) protein is the only phosphorylated structural protein of the coronavirus Transmissible gastroenteritis virus (TGEV). The phosphorylation state and intracellular distribution of TGEV N protein in infected cells were characterized by a combination of techniques including: (i) subcellular fractionation and analysis of tryptic peptides by two-dimensional nano-liquid chromatography, coupled to ion-trap mass spectrometry; (ii) tandem mass-spectrometry analysis of N protein resolved by SDS-PAGE; (iii) Western blotting using two specific antisera for phosphoserine-containing motif

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4

Lees-Miller, S. P., K. Sakaguchi, S. J. Ullrich, E. Appella, and C. W. Anderson. "Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53." Molecular and Cellular Biology 12, no. 11 (1992): 5041–49. http://dx.doi.org/10.1128/mcb.12.11.5041.

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Human DNA-PK is a nuclear, serine/threonine protein kinase that, when activated by DNA, phosphorylates several DNA-binding substrates, including the tumor suppressor protein p53. To identify which p53 residues are phosphorylated, we examined DNA-PK's ability to phosphorylate synthetic peptides corresponding to human p53 sequences. Serines 15 and 37 in the amino-terminal transactivation domain of human p53, and serines 7 and 18 of mouse p53, were phosphorylated by DNA-PK in the context of synthetic peptides. Other serines in these p53 peptides, and serines in other p53 peptides, including pepti

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5

Lees-Miller, S. P., K. Sakaguchi, S. J. Ullrich, E. Appella, and C. W. Anderson. "Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53." Molecular and Cellular Biology 12, no. 11 (1992): 5041–49. http://dx.doi.org/10.1128/mcb.12.11.5041-5049.1992.

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Human DNA-PK is a nuclear, serine/threonine protein kinase that, when activated by DNA, phosphorylates several DNA-binding substrates, including the tumor suppressor protein p53. To identify which p53 residues are phosphorylated, we examined DNA-PK's ability to phosphorylate synthetic peptides corresponding to human p53 sequences. Serines 15 and 37 in the amino-terminal transactivation domain of human p53, and serines 7 and 18 of mouse p53, were phosphorylated by DNA-PK in the context of synthetic peptides. Other serines in these p53 peptides, and serines in other p53 peptides, including pepti

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6

Navarro-García, Fernando, Adrián Canizalez-Roman, Bao Quan Sui, James P. Nataro, and Yenia Azamar. "The Serine Protease Motif of EspC from Enteropathogenic Escherichia coli Produces Epithelial Damage by a Mechanism Different from That of Pet Toxin from Enteroaggregative E. coli." Infection and Immunity 72, no. 6 (2004): 3609–21. http://dx.doi.org/10.1128/iai.72.6.3609-3621.2004.

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ABSTRACT EspC (Escherichia coli secreted protein C) of enteropathogenic E. coli (EPEC) shows the three classical domains of the autotransporter proteins and has a conserved serine protease motif belonging to the SPATE (serine protease autotransporters of Enterobacteriaceae) subfamily. EspC and its homolog Pet in enteroaggregative E. coli (EAEC) bear the same sequence within the serine protease motif, and both proteins produce enterotoxic effects, suggesting that like Pet, EspC could be internalized to reach and cleave the calmodulin-binding domain of fodrin, causing actin cytoskeleton disrupti

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7

Melegari, Margherita, Sarah K. Wolf, and Robert J. Schneider. "Hepatitis B Virus DNA Replication Is Coordinated by Core Protein Serine Phosphorylation and HBx Expression." Journal of Virology 79, no. 15 (2005): 9810–20. http://dx.doi.org/10.1128/jvi.79.15.9810-9820.2005.

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ABSTRACT The hepatitis B virus (HBV) core protein forms the capsid of viral particles and is essential for viral genome DNA replication and maturation. The C terminus of core protein contains three serines at positions 155, 162, and 170, phosphorylation of which is important for viral DNA replication. We demonstrate that the phosphorylation of these serines is stimulated by the viral HBx protein, a regulatory protein that activates signal transduction pathways and viral replication. HBx is therefore shown to stimulate HBV replication by increasing core serine phosphorylation. Mutational, bioch

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8

Koehler, Christian J., and Bernd Thiede. "Predominant cleavage of proteins N-terminal to serines and threonines using scandium(III) triflate." JBIC Journal of Biological Inorganic Chemistry 25, no. 1 (2019): 61–66. http://dx.doi.org/10.1007/s00775-019-01733-7.

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Abstract Proteolytic digestion prior to LC–MS analysis is a key step for the identification of proteins. Digestion of proteins is typically performed with trypsin, but certain proteins or important protein sequence regions might be missed using this endoproteinase. Only few alternative endoproteinases are available and chemical cleavage of proteins is rarely used. Recently, it has been reported that some metal complexes can act as artificial proteases. In particular, the Lewis acid scandium(III) triflate has been shown to catalyze the cleavage of peptide bonds to serine and threonine residues.

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9

Yi, Xian Ping, Jibin Zhou, Lu Huber, et al. "Nuclear compartmentalization of FAK and FRNK in cardiac myocytes." American Journal of Physiology-Heart and Circulatory Physiology 290, no. 6 (2006): H2509—H2515. http://dx.doi.org/10.1152/ajpheart.00659.2005.

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Focal adhesion kinase (FAK) and FAK-related non-kinase (FRNK) accumulate in the nucleus of cardiac myocytes during hypertensive hypertrophy. Nuclear FAK and FRNK are phosphorylated on different serines and form distinct bright spots. The subnuclear distribution of serine-phosphorylated FAK and FRNK was examined in this study by double labeling with fibrillarin, a component of nucleoli, and Sam68, a constituent of Sam68 nuclear bodies. We also investigated the role of protein kinase C (PKC)-mediated phosphorylation of FAK and FRNK on nuclear translocation. PKC activation by 12- O-tetradecanoylp

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10

DaSilva, John, Lizhong Xu, Hong Joo Kim, W. Todd Miller, and Dafna Bar-Sagi. "Regulation of Sprouty Stability by Mnk1-Dependent Phosphorylation." Molecular and Cellular Biology 26, no. 5 (2006): 1898–907. http://dx.doi.org/10.1128/mcb.26.5.1898-1907.2006.

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ABSTRACT Sprouty (Spry) proteins are negative feedback modulators of receptor tyrosine kinase pathways in Drosophila melanogaster and mammals. Mammalian Spry proteins have been shown to undergo tyrosine and serine phosphorylation in response to growth factor stimulation. While several studies have addressed the function of tyrosine phosphorylation of Spry, little is known about the significance of Spry serine phosphorylation. Here we identify mitogen-activated protein kinase-interacting kinase 1 (Mnk1) as the kinase that phosphorylates human Spry2 (hSpry2) on serines 112 and 121. Mutation of t

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11

Wang, C. Y., S. C. Ku, C. C. Lee, and A. H. J. Wang. "Modulating the function of human serine racemase and human serine dehydratase by protein engineering." Protein Engineering Design and Selection 25, no. 11 (2012): 741–49. http://dx.doi.org/10.1093/protein/gzs078.

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12

Cartee, Tara L., and Gail W. Wertz. "Respiratory Syncytial Virus M2-1 Protein Requires Phosphorylation for Efficient Function and Binds Viral RNA during Infection." Journal of Virology 75, no. 24 (2001): 12188–97. http://dx.doi.org/10.1128/jvi.75.24.12188-12197.2001.

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ABSTRACT The M2-1 protein of respiratory syncytial (RS) virus is a transcriptional processivity and antitermination factor. The M2-1 protein has a Cys3His1 zinc binding motif which is essential for function, is phosphorylated, and has been shown to interact with the RS virus nucleocapsid (N) protein. In the work reported here, we determined the sites at which the M2-1 protein was phosphorylated and investigated the importance of these phosphorylated residues for M2-1 function in transcription. By combining protease digestion, matrix-assisted laser desorption ionization–time of flight mass spec

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13

Freeman, R. S., A. N. Meyer, J. Li, and D. J. Donoghue. "Phosphorylation of conserved serine residues does not regulate the ability of mosxe protein kinase to induce oocyte maturation or function as cytostatic factor." Journal of Cell Biology 116, no. 3 (1992): 725–35. http://dx.doi.org/10.1083/jcb.116.3.725.

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Expression of the mosxe protein kinase is required for the normal meiotic maturation of Xenopus oocytes and overexpression induces maturation in the absence of other stimuli. In addition, mosxe functions as a component of cytostatic factor (CSF), an activity responsible for arrest of the mature egg at metaphase II. After microinjection of Xenopus oocytes with in vitro synthesized RNA encoding either wild-type mosxe or kinase-inactive mosxe(R90), both proteins are phosphorylated exclusively on serine residues and exhibit essentially identical chymotryptic maps. Since the phosphorylated kinase-i

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14

Gegenbauer, Kristina, Giuliano Elia, Alfonso Blanco-Fernandez, and Albert Smolenski. "Regulator of G-protein signaling 18 integrates activating and inhibitory signaling in platelets." Blood 119, no. 16 (2012): 3799–807. http://dx.doi.org/10.1182/blood-2011-11-390369.

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Abstract Regulator of G-protein signaling 18 (RGS18) is a GTPase-activating protein for the G-α-q and G-α-i subunits of heterotrimeric G-proteins that turns off signaling by G-protein coupled receptors. RGS18 is highly expressed in platelets. In the present study, we show that the 14-3-3γ protein binds to phosphorylated serines 49 and 218 of RGS18. Platelet activation by thrombin, thromboxane A2, or ADP stimulates the association of 14-3-3 and RGS18, probably by increasing the phosphorylation of serine 49. In contrast, treatment of platelets with prostacyclin and nitric oxide, which trigger in

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15

Benkhelifa, Sofia, Sylvain Provot, Eugène Nabais, Alain Eychène, Georges Calothy, and Marie-Paule Felder-Schmittbuhl. "Phosphorylation of MafA Is Essential for Its Transcriptional and Biological Properties." Molecular and Cellular Biology 21, no. 14 (2001): 4441–52. http://dx.doi.org/10.1128/mcb.21.14.4441-4452.2001.

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ABSTRACT We previously described the identification of quail MafA, a novel transcription factor of the Maf bZIP (basic region leucine zipper) family, expressed in the differentiating neuroretina (NR). In the present study, we provide the first evidence that MafA is phosphorylated and that its biological properties strongly rely upon phosphorylation of serines 14 and 65, two residues located in the transcriptional activating domain within a consensus for phosphorylation by mitogen-activated protein kinases and which are conserved among Maf proteins. These residues are phosphorylated by ERK2 but

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16

Li, Xuejun, Claire Halpin, and Martin D. Ryan. "A novel cleavage site within the potato leafroll virus P1 polyprotein." Journal of General Virology 88, no. 5 (2007): 1620–23. http://dx.doi.org/10.1099/vir.0.82627-0.

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To study the proteolytic processing of the potato leafroll virus replicase proteins, the multidomain P1 protein with a c-myc epitope tag attached at the N terminus was expressed in insect cells by using the baculovirus system. Western blotting showed that P1 was cleaved at a site upstream of the serine protease domain, in addition to the cleavage site downstream of the protease domain. Mutational analysis showed that the serine protease domain within P1 was responsible for this cleavage. To characterize this novel cleavage site further, a portion of the P1 protein comprising the protease domai

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Im, H., M. J. Ryu, and M. H. Yu. "Engineering thermostability in serine protease inhibitors." Protein Engineering Design and Selection 17, no. 4 (2004): 325–31. http://dx.doi.org/10.1093/protein/gzh036.

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18

Patel, Seema K., Jimmie Dotson, Kenneth P. Allen, and James M. Fleckenstein. "Identification and Molecular Characterization of EatA, an Autotransporter Protein of Enterotoxigenic Escherichia coli." Infection and Immunity 72, no. 3 (2004): 1786–94. http://dx.doi.org/10.1128/iai.72.3.1786-1794.2004.

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ABSTRACT Enterotoxigenic Escherichia coli (ETEC) strains remain a formidable cause of diarrheal disease. To identify novel surface proteins of ETEC, we performed TnphoA mutagenesis of prototype ETEC strain H10407 and discovered a secreted protein not previously recognized in ETEC. DNA sequencing of the interrupted locus in mutant TnphoA.977 revealed a candidate 4,095-bp open reading frame without significant homology to commensal E. coli K-12 genomic DNA. Translation of this sequence revealed that it encoded a predicted peptide of 147.7 kDa that bears significant homology to members of the aut

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19

Kostakioti, Maria, and Christos Stathopoulos. "Functional Analysis of the Tsh Autotransporter from an Avian Pathogenic Escherichia coli Strain." Infection and Immunity 72, no. 10 (2004): 5548–54. http://dx.doi.org/10.1128/iai.72.10.5548-5554.2004.

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ABSTRACT The temperature-sensitive hemagglutinin (Tsh) is an autotransporter protein secreted by avian-pathogenic Escherichia coli strains that colonize the respiratory tract and lead to airsacculitis, pericarditis, and colisepticemia. It is synthesized as a 140-kDa precursor protein, whose processing results in a 106-kDa passenger domain (Tshs) and a 33-kDa β-domain (Tshβ). The presence of a conserved 7-amino-acid serine protease motif within Tshs classifies the protein in a subfamily of autotransporters, known as serine protease autotransporters of the Enterobacteriaceae. In this study, we r

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Neidel, Sarah, Hongwei Ren, Alice A. Torres та Geoffrey L. Smith. "NF-κB activation is a turn on for vaccinia virus phosphoprotein A49 to turn off NF-κB activation". Proceedings of the National Academy of Sciences 116, № 12 (2019): 5699–704. http://dx.doi.org/10.1073/pnas.1813504116.

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Vaccinia virus protein A49 inhibits NF-κB activation by molecular mimicry and has a motif near the N terminus that is conserved in IκBα, β-catenin, HIV Vpu, and some other proteins. This motif contains two serines, and for IκBα and β-catenin, phosphorylation of these serines enables recognition by the E3 ubiquitin ligase β-TrCP. Binding of IκBα and β-catenin by β-TrCP causes their ubiquitylation and thereafter proteasome-mediated degradation. In contrast, HIV Vpu and VACV A49 are not degraded. This paper shows that A49 is phosphorylated at serine 7 but not serine 12 and that this is necessary

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Rice, Kelly, Robert Peralta, Darrin Bast, Joyce de Azavedo, and Martin J. McGavin. "Description of Staphylococcus Serine Protease (ssp) Operon in Staphylococcus aureus and Nonpolar Inactivation of sspA-Encoded Serine Protease." Infection and Immunity 69, no. 1 (2001): 159–69. http://dx.doi.org/10.1128/iai.69.1.159-169.2001.

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ABSTRACT Signature tagged mutagenesis has recently revealed that the Ssp serine protease (V8 protease) contributes to in vivo growth and survival of Staphylococcus aureus in different infection models, and our previous work indicated that Ssp could play a role in controlling microbial adhesion. In this study, we describe an operon structure within the ssp locus of S. aureusRN6390. The ssp gene encoding V8 protease is designated assspA, and is followed by sspB, which encodes a 40.6-kDa cysteine protease, and sspC, which encodes a 12.9-kDa protein of unknown function. S. aureus SP6391 is an isog

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Inuzuka, Madoka, Minako Hayakawa, and Tatsuya Ingi. "Serinc, an Activity-regulated Protein Family, Incorporates Serine into Membrane Lipid Synthesis." Journal of Biological Chemistry 280, no. 42 (2005): 35776–83. http://dx.doi.org/10.1074/jbc.m505712200.

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23

Otlewski, J., D. Krowarsch, and W. Apostoluk. "Protein inhibitors of serine proteinases." Acta Biochimica Polonica 46, no. 3 (1999): 531–65. http://dx.doi.org/10.18388/abp.1999_4128.

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Serine proteinases and their natural protein inhibitors belong to the most intensively studied models of protein-protein recognition. Protein inhibitors do not form a single group but can be divided into about 20 different families. Global structures of proteins representing different inhibitor families are completely different and comprise alpha-helical proteins, beta-sheet proteins, alpha/beta-proteins and different folds of small disulfide-rich proteins. Three different types of inhibitors can be distinguished: canonical (standard mechanism) inhibitors, non-canonical inhibitors, and serpins

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Milano, Teresa, Martino Luigi Di Salvo, Sebastiana Angelaccio, and Stefano Pascarella. "Conserved water molecules in bacterial serine hydroxymethyltransferases." Protein Engineering Design and Selection 28, no. 10 (2015): 415–26. http://dx.doi.org/10.1093/protein/gzv026.

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Nabian, Sedigheh, Mohammad Taheri, Mohammad Mehdi Ranjbar, Alireza Sazmand, Parastou Youssefy, and Gholam Reza Nazaralipour. "Assessment and partial purification of serine protease inhibitors from Rhipicephalus (Boophilus) annulatuslarvae." Revista Brasileira de Parasitologia Veterinária 23, no. 2 (2014): 187–93. http://dx.doi.org/10.1590/s1984-29612014036.

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Ticks are rich sources of serine protease inhibitors, particularly those that prevent blood clotting and inflammatory responses during blood feeding. The tick Rhipicephalus (Boophlus) annulatusis an important ectoparasite of cattle. The aims of this study were to characterize and purify the serine protease inhibitors present in R. (B.) annulatus larval extract. The inhibitors were characterized by means of one and two-dimensional reverse zymography, and purified using affinity chromatography on a trypsin-Sepharose column. The analysis on one and two-dimensional reverse zymography of the larval

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Karlsson, Anna, Patricia Saravia-Otten, Karin Tegmark, Eva Morfeldt, and Staffan Arvidson. "Decreased Amounts of Cell Wall-Associated Protein A and Fibronectin-Binding Proteins in Staphylococcus aureus sarA Mutants due to Up-Regulation of Extracellular Proteases." Infection and Immunity 69, no. 8 (2001): 4742–48. http://dx.doi.org/10.1128/iai.69.8.4742-4748.2001.

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ABSTRACT Data have been presented indicating that Staphylococcus aureus cell surface protein can be degraded by extracellular proteases produced by the same bacterium. We have found that insarA mutant cells, which produce high amounts of four major extracellular proteases (staphylococcal serine protease [V8 protease] [SspA], cysteine protease [SspB], aureolysin [metalloprotease] [Aur], and staphopain [Scp]), the levels of cell-bound fibronectin-binding proteins (FnBPs) and protein A were very low compared to those of wild-type cells, in spite of unaltered or increased transcription of the corr

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27

Tratner, I., R. Ofir, and I. M. Verma. "Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential." Molecular and Cellular Biology 12, no. 3 (1992): 998–1006. http://dx.doi.org/10.1128/mcb.12.3.998.

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We have studied the phosphorylation of the nuclear oncoprotein Fos by cyclic AMP-dependent protein kinase (PKA). We demonstrate that the human c-Fos protein, phosphorylated either in vitro with purified PKA or in vivo in JEG3 cells following treatment with forskolin, has similar phosphotryptic peptide maps. Serine 362, which constitutes part of a canonical PKA phosphorylation site (RKGSSS), is phosphorylated both in vivo and in vitro. A mutant of Fos protein in which serine residues 362 to 364 have been altered to alanine residues is not efficiently phosphorylated in vitro. Furthermore, Fos pr

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Tratner, I., R. Ofir, and I. M. Verma. "Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential." Molecular and Cellular Biology 12, no. 3 (1992): 998–1006. http://dx.doi.org/10.1128/mcb.12.3.998-1006.1992.

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We have studied the phosphorylation of the nuclear oncoprotein Fos by cyclic AMP-dependent protein kinase (PKA). We demonstrate that the human c-Fos protein, phosphorylated either in vitro with purified PKA or in vivo in JEG3 cells following treatment with forskolin, has similar phosphotryptic peptide maps. Serine 362, which constitutes part of a canonical PKA phosphorylation site (RKGSSS), is phosphorylated both in vivo and in vitro. A mutant of Fos protein in which serine residues 362 to 364 have been altered to alanine residues is not efficiently phosphorylated in vitro. Furthermore, Fos pr

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Du, Min, Robert L. S. Perry, Nathaniel B. Nowacki, et al. "Protein Kinase A Represses Skeletal Myogenesis by Targeting Myocyte Enhancer Factor 2D." Molecular and Cellular Biology 28, no. 9 (2008): 2952–70. http://dx.doi.org/10.1128/mcb.00248-08.

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ABSTRACT Activation of protein kinase A (PKA) by elevation of the intracellular cyclic AMP (cAMP) level inhibits skeletal myogenesis. Previously, an indirect modulation of the myogenic regulatory factors (MRFs) was implicated as the mechanism. Because myocyte enhancer factor 2 (MEF2) proteins are key regulators of myogenesis and obligatory partners for the MRFs, here we assessed whether these proteins could be involved in PKA-mediated myogenic repression. Initially, in silico analysis revealed several consensus PKA phosphoacceptor sites on MEF2, and subsequent analysis by in vitro kinase assay

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Brown, K., G. Franzoso, L. Baldi, et al. "The signal response of IkappaB alpha is regulated by transferable N- and C-terminal domains." Molecular and Cellular Biology 17, no. 6 (1997): 3021–27. http://dx.doi.org/10.1128/mcb.17.6.3021.

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IkappaB alpha retains the transcription factor NF-kappaB in the cytoplasm, thus inhibiting its function. Various stimuli inactivate IkappaB alpha by triggering phosphorylation of the N-terminal residues Ser32 and Ser36. Phosphorylation of both serines is demonstrated directly by phosphopeptide mapping utilizing calpain protease, which cuts approximately 60 residues from the N terminus, and by analysis of mutants lacking one or both serine residues. Phosphorylation is followed by rapid proteolysis, and the liberated NF-kappaB translocates to the nucleus, where it activates transcription of its

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Marchal, Christelle, Rosine Haguenauer-Tsapis, and Daniele Urban-Grimal. "A PEST-Like Sequence Mediates Phosphorylation and Efficient Ubiquitination of Yeast Uracil Permease." Molecular and Cellular Biology 18, no. 1 (1998): 314–21. http://dx.doi.org/10.1128/mcb.18.1.314.

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ABSTRACT Uptake of uracil by the yeast Saccharomyces cerevisiaeis mediated by a specific permease encoded by the FUR4gene. Uracil permease located at the cell surface is subject to two covalent modifications: phosphorylation and ubiquitination. The ubiquitination step is necessary prior to permease endocytosis and subsequent vacuolar degradation. Here, we demonstrate that a PEST-like sequence located within the cytoplasmic N terminus of the protein is essential for uracil permease turnover. Internalization of the transporter was reduced when some of the serines within the region were converted

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Fernández-Abalos, José M., Verónica Reviejo, Margarita Díaz, Sonia Rodríguez, Fernando Leal, and Ramón I. Santamaría. "Posttranslational processing of the xylanase Xys1L from Streptomyces halstedii JM8 is carried out by secreted serine proteases." Microbiology 149, no. 7 (2003): 1623–32. http://dx.doi.org/10.1099/mic.0.26113-0.

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The xylanase Xys1L from Streptomyces halstedii JM8 is known to be processed extracellularly, to produce a protein of 33·7 kDa, Xys1S, that retains catalytic activity but not its cellulose-binding capacity. This paper demonstrates that at least five serine proteases isolated from Streptomyces spp. have the ability to process the xylanase Xys1L. The genes of two of these extracellular serine proteases, denominated SpB and SpC, were cloned from Streptomyces lividans 66 (a strain commonly used as a host for protein secretion), sequenced, and overexpressed in S. lividans; both purified proteases we

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Kwon, B. S., D. Kestler, E. Lee, M. Wakulchik, and J. D. Young. "Isolation and sequence analysis of serine protease cDNAs from mouse cytolytic T lymphocytes." Journal of Experimental Medicine 168, no. 5 (1988): 1839–54. http://dx.doi.org/10.1084/jem.168.5.1839.

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Three new cDNA clones (designated MCSP-1, MCSP-2, and MCSP-3) encoding mouse serine proteases were isolated from cloned cytolytic T lymphocytes (CTL) by a modified differential screening procedure. The putative mature proteins of MCSP-2 and MCSP-3 are each composed of 228 amino acids with molecular weights of 25,477 and 25,360, respectively. NH2-terminal amino acids of MCSP-2- and MCSP-3-predicted proteins were identical to those reported for granzyme E and F, respectively. The third species, MCSP-1, was closely related to the two other cDNA species but approximately 30 amino acids equivalents

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Ronaghan, Natalie J., Judie Shang, Vadim Iablokov, et al. "The serine protease-mediated increase in intestinal epithelial barrier function is dependent on occludin and requires an intact tight junction." American Journal of Physiology-Gastrointestinal and Liver Physiology 311, no. 3 (2016): G466—G479. http://dx.doi.org/10.1152/ajpgi.00441.2015.

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Barrier dysfunction is a characteristic of the inflammatory bowel diseases (IBD), Crohn's disease and ulcerative colitis. Understanding how the tight junction is modified to maintain barrier function may provide avenues for treatment of IBD. We have previously shown that the apical addition of serine proteases to intestinal epithelial cell lines causes a rapid and sustained increase in transepithelial electrical resistance (TER), but the mechanisms are unknown. We hypothesized that serine proteases increase barrier function through trafficking and insertion of tight junction proteins into the

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Manak, J. R., and R. Prywes. "Mutation of serum response factor phosphorylation sites and the mechanism by which its DNA-binding activity is increased by casein kinase II." Molecular and Cellular Biology 11, no. 7 (1991): 3652–59. http://dx.doi.org/10.1128/mcb.11.7.3652.

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Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro. We report here that serine 83 appears to be the residue phosphorylated by CKII but that three other serines in this region can also be involved in phosphorylation and the enhancement of DNA-binding activity. A mutant that contained glutamate residues in place of these serines had only low-level binding activity; however, when the serines were replace

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Manak, J. R., and R. Prywes. "Mutation of serum response factor phosphorylation sites and the mechanism by which its DNA-binding activity is increased by casein kinase II." Molecular and Cellular Biology 11, no. 7 (1991): 3652–59. http://dx.doi.org/10.1128/mcb.11.7.3652-3659.1991.

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Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro. We report here that serine 83 appears to be the residue phosphorylated by CKII but that three other serines in this region can also be involved in phosphorylation and the enhancement of DNA-binding activity. A mutant that contained glutamate residues in place of these serines had only low-level binding activity; however, when the serines were replace

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Wilkinson, D. J., T. V. Strong, M. K. Mansoura, et al. "CFTR activation: additive effects of stimulatory and inhibitory phosphorylation sites in the R domain." American Journal of Physiology-Lung Cellular and Molecular Physiology 273, no. 1 (1997): L127—L133. http://dx.doi.org/10.1152/ajplung.1997.273.1.l127.

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To investigate the functional significance of individual consensus phosphorylation sites within the R domain of cystic fibrosis transmembrane conductance regulator (CFTR), serines were eliminated by substituting them with alanine. Included in this analysis were serine-660, -670, -686, -700, -712, -737, -768, -795, and -813, which lie within protein kinase A consensus sequences, and serine-641, which does not. Elimination of single potential phosphorylation sites altered the sensitivity of CFTR (expressed in Xenopus oocytes) to activating conditions in a manner that was highly site dependent. S

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Knudsen, E. S., and J. Y. Wang. "Dual mechanisms for the inhibition of E2F binding to RB by cyclin-dependent kinase-mediated RB phosphorylation." Molecular and Cellular Biology 17, no. 10 (1997): 5771–83. http://dx.doi.org/10.1128/mcb.17.10.5771.

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The growth suppression function of RB is dependent on its protein binding activity. RB contains at least three distinct protein binding functions: (i) the A/B pocket, which binds proteins with the LXCXE motif; (ii) the C pocket, which binds the c-Abl tyrosine kinase; and (iii) the large A/B pocket, which binds the E2F family of transcription factors. Phosphorylation of RB, which is catalyzed by cyclin-dependent protein kinases, inhibits all three protein binding activities. We have previously shown that LXCXE binding is inactivated by the phosphorylation of two threonines (Thr821 and Thr826),

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Ward, Y., B. Spinelli, M. J. Quon, H. Chen, S. R. Ikeda, and K. Kelly. "Phosphorylation of Critical Serine Residues in Gem Separates Cytoskeletal Reorganization from Down-Regulation of Calcium Channel Activity." Molecular and Cellular Biology 24, no. 2 (2004): 651–61. http://dx.doi.org/10.1128/mcb.24.2.651-661.2004.

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ABSTRACT Gem is a small GTP-binding protein that has a ras-like core and extended chains at each terminus. The primary structure of Gem and other RGK family members (Rad, Rem, and Rem2) predicts a GTPase deficiency, leading to the question of how Gem functional activity is regulated. Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium chann

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Peng, RongSheng, Jie Tan, and Paul D. Ling. "Conserved Regions in the Epstein-Barr Virus Leader Protein Define Distinct Domains Required for Nuclear Localization and Transcriptional Cooperation with EBNA2." Journal of Virology 74, no. 21 (2000): 9953–63. http://dx.doi.org/10.1128/jvi.74.21.9953-9963.2000.

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ABSTRACT Epstein-Barr virus (EBV) EBNA-LP is a latent protein whose function is not fully understood. Recent studies have shown that EBNA-LP may be an important EBNA2 cofactor by enhancing EBNA2 stimulation of the latency C and LMP-1 promoters. To further our understanding of EBNA-LP function, we have introduced a series of mutations into evolutionarily conserved regions and tested the mutant proteins for the ability to enhance EBNA2 stimulation of the latency C and LMP-1 promoters. Three conserved regions (CR1 to CR3) are located in the repeat domains that are essential for the EBNA2 cooperat

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Clement, Herlinda, Ligia Luz Corrales-García, Damaris Bolaños, Gerardo Corzo, and Elba Villegas. "Immunogenic Properties of Recombinant Enzymes from Bothrops ammodytoides towards the Generation of Neutralizing Antibodies against Its Own Venom." Toxins 11, no. 12 (2019): 702. http://dx.doi.org/10.3390/toxins11120702.

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Bothropic venoms contain enzymes such as metalloproteases, serine-proteases, and phospholipases, which acting by themselves, or in synergism, are the cause of the envenomation symptoms and death. Here, two mRNA transcripts, one that codes for a metalloprotease and another for a serine-protease, were isolated from a Bothrops ammodytoides venom gland. The metalloprotease and serine-protease transcripts were cloned on a pCR®2.1-TOPO vector and consequently expressed in a recombinant way in E. coli (strains Origami and M15, respectively), using pQE30 vectors. The recombinant proteins were named rB

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Vostrov, Alexander A., and Wolfgang W. Quitschke. "Plasma Hyaluronan-binding Protein Is a Serine Protease." Journal of Biological Chemistry 275, no. 30 (2000): 22978–85. http://dx.doi.org/10.1074/jbc.m904640199.

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Lin, Ming-Huei, Robert Kuo-Kuang Lee, Yuh-Ming Hwu, et al. "SPINKL, a Kazal-type serine protease inhibitor-like protein purified from mouse seminal vesicle fluid, is able to inhibit sperm capacitation." REPRODUCTION 136, no. 5 (2008): 559–71. http://dx.doi.org/10.1530/rep-07-0375.

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We report a secreted serine protease inhibitor Kazal-type-like (SPINKL) protein. The SPINKL protein was purified from mouse seminal vesicle secretions through a series of steps, including ion-exchange chromatography on a diethylaminoethyl-Sephacel column, gel filtration on a Sephadex G-75 column, and ion-exchange HPLC on a Q strong anion exchange column. Further analysis identified several SPINKL proteins with various N-linked carbohydrates. The SPINKL protein has six conserved cysteine residues that are nearly identical to those of members of the SPINK protein family. It was noted that the SP

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Spiridonova, V. A. "Molecular recognition elements - DNA/RNA-aptamers to proteins." Biomeditsinskaya Khimiya 56, no. 6 (2010): 639–56. http://dx.doi.org/10.18097/pbmc20105606639.

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In this review summarizes data on DNA/RNA aptamers - a novel class of molecular recognition elements. Special attention is paid to the aptamers to proteins involved into pathogenesis of wide spread human diseases. These include aptamers to serine protease, to cytokines/growth factors, to influenza viral protein, nucleic acid binding proteins. Strong and specific binding for a given protein target of aptamers make them an attractive class of direct protein inhibitors. They can inhibit pathogenic proteins and it is becoming clear that aptamers have the potential to be a new and effective class o

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Rojas, Santos, Kara A. Corbin-Lickfett, Laurimar Escudero-Paunetto, and Rozanne M. Sandri-Goldin. "ICP27 Phosphorylation Site Mutants Are Defective in Herpes Simplex Virus 1 Replication and Gene Expression." Journal of Virology 84, no. 5 (2009): 2200–2211. http://dx.doi.org/10.1128/jvi.00917-09.

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ABSTRACT Herpes simplex virus 1 (HSV-1) protein ICP27 is a multifunctional regulatory protein that is posttranslationally modified by phosphorylation during viral infection. ICP27 has been shown to be phosphorylated on three serine residues, specifically serine residues 16 and 18, which are within casein kinase 2 (CK2) sites, and serine residue 114, which is within a protein kinase A (PKA) site. Phosphorylation is an important regulatory mechanism that is reversible and controls many signaling pathways, protein-protein interactions, and protein subcellular localization. To determine the role o

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Zahler, A. M., K. M. Neugebauer, J. A. Stolk, and M. B. Roth. "Human SR proteins and isolation of a cDNA encoding SRp75." Molecular and Cellular Biology 13, no. 7 (1993): 4023–28. http://dx.doi.org/10.1128/mcb.13.7.4023.

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SR proteins are a family of proteins that have a common epitope recognized by a monoclonal antibody (MAb104) that binds active sites of polymerase II transcription. Four of the SR family members have been shown to restore activity to an otherwise splicing-deficient extract (S100 extract). Here we show that two untested SR proteins, SRp20 and SRp75, can also complement the splicing-deficient extract. We isolated a cDNA encoding SRp75 and found that this protein, like other SR proteins, contains an N-terminal RNA recognition motif (RRM), a glycine-rich region, an internal region homologous to th

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Zahler, A. M., K. M. Neugebauer, J. A. Stolk, and M. B. Roth. "Human SR proteins and isolation of a cDNA encoding SRp75." Molecular and Cellular Biology 13, no. 7 (1993): 4023–28. http://dx.doi.org/10.1128/mcb.13.7.4023-4028.1993.

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SR proteins are a family of proteins that have a common epitope recognized by a monoclonal antibody (MAb104) that binds active sites of polymerase II transcription. Four of the SR family members have been shown to restore activity to an otherwise splicing-deficient extract (S100 extract). Here we show that two untested SR proteins, SRp20 and SRp75, can also complement the splicing-deficient extract. We isolated a cDNA encoding SRp75 and found that this protein, like other SR proteins, contains an N-terminal RNA recognition motif (RRM), a glycine-rich region, an internal region homologous to th

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MacPherson, Matthew Reid, Patricia Molina, Serhiy Souchelnytskyi, et al. "Phosphorylation of Serine 11 and Serine 92 as New Positive Regulators of Human Snail1 Function: Potential Involvement of Casein Kinase-2 and the cAMP-activated Kinase Protein Kinase A." Molecular Biology of the Cell 21, no. 2 (2010): 244–53. http://dx.doi.org/10.1091/mbc.e09-06-0504.

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Snail1 is a major factor for epithelial-mesenchymal transition (EMT), an important event in tumor metastasis and in other pathologies. Snail1 is tightly regulated at transcriptional and posttranscriptional levels. Control of Snail1 protein stability and nuclear export by GSK3β phosphorylation is important for Snail1 functionality. Stabilization mechanisms independent of GSK3β have also been reported, including interaction with LOXL2 or regulation of the COP9 signalosome by inflammatory signals. To get further insights into the role of Snail1 phosphorylation, we have performed an in-depth analy

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Turner, David P. J., Karl G. Wooldridge, and Dlawer A. A. Ala'Aldeen. "Autotransported Serine Protease A of Neisseria meningitidis: an Immunogenic, Surface-Exposed Outer Membrane, and Secreted Protein." Infection and Immunity 70, no. 8 (2002): 4447–61. http://dx.doi.org/10.1128/iai.70.8.4447-4461.2002.

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ABSTRACT Several autotransporter proteins have previously been identified in Neisseria meningitidis. Using molecular features common to most members of the autotransporter family of proteins, we have identified an additional novel ca. 112-kDa autotransporter protein in the meningococcal genomic sequence data. This protein, designated autotransported serine protease A (AspA), has significant N-terminal homology to the secreted serine proteases (subtilases) from several organisms and contains a serine protease catalytic triad. The amino acid sequence of AspA is well-conserved in serogroup A, B,

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Tegmark, Karin, Eva Morfeldt, and Staffan Arvidson. "Regulation of agr-Dependent Virulence Genes in Staphylococcus aureus by RNAIII from Coagulase-Negative Staphylococci." Journal of Bacteriology 180, no. 12 (1998): 3181–86. http://dx.doi.org/10.1128/jb.180.12.3181-3186.1998.

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ABSTRACT Many of the genes coding for extracellular toxins, enzymes, and cell surface proteins in Staphylococcus aureus are regulated by a 510-nucleotide (nt) RNA molecule, RNAIII. Transcription of genes encoding secreted toxins and enzymes, includinghla (alpha-toxin), saeB (enterotoxin B),tst (toxic shock syndrome toxin 1), and ssp(serine protease), is stimulated, while transcription of genes encoding cell surface proteins, like spa (protein A) andfnb (fibronectin binding proteins), is repressed. Besides being a regulator, RNAIII is also an mRNA coding for staphylococcal delta-lysin. We have

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