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Relevant bibliographies by topics / Molecular chaperone DnaK

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Academic literature on the topic 'Molecular chaperone DnaK'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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Journal articles on the topic "Molecular chaperone DnaK"

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Silberg, Jonathan J., Kevin G. Hoff, and Larry E. Vickery. "The Hsc66-Hsc20 Chaperone System inEscherichia coli: Chaperone Activity and Interactions with the DnaK-DnaJ-GrpE System." Journal of Bacteriology 180, no. 24 (1998): 6617–24. http://dx.doi.org/10.1128/jb.180.24.6617-6624.1998.

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ABSTRACT Hsc66, a stress-70 protein, and Hsc20, a J-type accessory protein, comprise a newly described Hsp70-type chaperone system in addition to DnaK-DnaJ-GrpE in Escherichia coli. Because endogenous substrates for the Hsc66-Hsc20 system have not yet been identified, we investigated chaperone-like activities of Hsc66 and Hsc20 by their ability to suppress aggregation of denatured model substrate proteins, such as rhodanese, citrate synthase, and luciferase. Hsc66 suppressed aggregation of rhodanese and citrate synthase, and ATP caused effects consistent with complex destabilization typical of

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Acebrón, Sergio P., Vanesa Fernández-Sáiz, Stefka G. Taneva, Fernando Moro, and Arturo Muga. "DnaJ Recruits DnaK to Protein Aggregates." Journal of Biological Chemistry 283, no. 3 (2007): 1381–90. http://dx.doi.org/10.1074/jbc.m706189200.

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Thermal stress might lead to protein aggregation in the cell. Reactivation of protein aggregates depends on Hsp100 and Hsp70 chaperones. We focus in this study on the ability of DnaK, the bacterial representative of the Hsp70 family, to interact with different aggregated model substrates. Our data indicate that DnaK binding to large protein aggregates is mediated by DnaJ, and therefore it depends on its affinity for the cochaperone. Mutations in the structural region of DnaK known as the “latch” decrease the affinity of the chaperone for DnaJ, resulting in a defective activity as protein aggre

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Susin, Michelle F., Regina L. Baldini, Frederico Gueiros-Filho, and Suely L. Gomes. "GroES/GroEL and DnaK/DnaJ Have Distinct Roles in Stress Responses and during Cell Cycle Progression in Caulobacter crescentus." Journal of Bacteriology 188, no. 23 (2006): 8044–53. http://dx.doi.org/10.1128/jb.00824-06.

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ABSTRACT Misfolding and aggregation of protein molecules are major threats to all living organisms. Therefore, cells have evolved quality control systems for proteins consisting of molecular chaperones and proteases, which prevent protein aggregation by either refolding or degrading misfolded proteins. DnaK/DnaJ and GroES/GroEL are the best-characterized molecular chaperone systems in bacteria. In Caulobacter crescentus these chaperone machines are the products of essential genes, which are both induced by heat shock and cell cycle regulated. In this work, we characterized the viabilities of c

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Macario, Alberto J. L., and Everly Conway de Macario. "The Archaeal Molecular Chaperone Machine: Peculiarities and Paradoxes." Genetics 152, no. 4 (1999): 1277–83. http://dx.doi.org/10.1093/genetics/152.4.1277.

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Abstract A major finding within the field of archaea and molecular chaperones has been the demonstration that, while some species have the stress (heat-shock) gene hsp70(dnaK), others do not. This gene encodes Hsp70(DnaK), an essential molecular chaperone in bacteria and eukaryotes. Due to the physiological importance and the high degree of conservation of this protein, its absence in archaeal organisms has raised intriguing questions pertaining to the evolution of the chaperone machine as a whole and that of its components in particular, namely, Hsp70(DnaK), Hsp40(DnaJ), and GrpE. Another arc

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Lin, Jiusheng, and Mark A. Wilson. "Escherichia coli Thioredoxin-like Protein YbbN Contains an Atypical Tetratricopeptide Repeat Motif and Is a Negative Regulator of GroEL." Journal of Biological Chemistry 286, no. 22 (2011): 19459–69. http://dx.doi.org/10.1074/jbc.m111.238741.

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Many proteins contain a thioredoxin (Trx)-like domain fused with one or more partner domains that diversify protein function by the modular construction of new molecules. The Escherichia coli protein YbbN is a Trx-like protein that contains a C-terminal domain with low homology to tetratricopeptide repeat motifs. YbbN has been proposed to act as a chaperone or co-chaperone that aids in heat stress response and DNA synthesis. We report the crystal structure of YbbN, which is an elongated molecule with a mobile Trx domain and four atypical tetratricopeptide repeat motifs. The Trx domain lacks a

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Lupoli, Tania J., Allison Fay, Carolina Adura, Michael S. Glickman, and Carl F. Nathan. "Reconstitution of aMycobacterium tuberculosisproteostasis network highlights essential cofactor interactions with chaperone DnaK." Proceedings of the National Academy of Sciences 113, no. 49 (2016): E7947—E7956. http://dx.doi.org/10.1073/pnas.1617644113.

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During host infection,Mycobacterium tuberculosis(Mtb) encounters several types of stress that impair protein integrity, including reactive oxygen and nitrogen species and chemotherapy. The resulting protein aggregates can be resolved or degraded by molecular machinery conserved from bacteria to eukaryotes. Eukaryotic Hsp104/Hsp70 and their bacterial homologs ClpB/DnaK are ATP-powered chaperones that restore toxic protein aggregates to a native folded state. DnaK is essential inMycobacterium smegmatis, and ClpB is involved in asymmetrically distributing damaged proteins during cell division as

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Zmijewski, Michał A., Joanna Skórko-Glonek, Fabio Tanfani, et al. "Structural basis of the interspecies interaction between the chaperone DnaK(Hsp70) and the co-chaperone GrpE of archaea and bacteria." Acta Biochimica Polonica 54, no. 2 (2007): 245–52. http://dx.doi.org/10.18388/abp.2007_3244.

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Hsp70s are chaperone proteins that are conserved in evolution and present in all prokaryotic and eukaryotic organisms. In the archaea, which form a distinct kingdom, the Hsp70 chaperones have been found in some species only, including Methanosarcina mazei. Both the bacterial and archaeal Hsp70(DnaK) chaperones cooperate with a GrpE co-chaperone which stimulates the ATPase activity of the DnaK protein. It is currently believed that the archaeal Hsp70 system was obtained by the lateral transfer of chaperone genes from bacteria. Our previous finding that the DnaK and GrpE proteins of M. mazei can

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Koch, Birgit, Mogens Kilstrup, Finn K. Vogensen, and Karin Hammer. "Induced Levels of Heat Shock Proteins in adnaK Mutant of Lactococcus lactis." Journal of Bacteriology 180, no. 15 (1998): 3873–81. http://dx.doi.org/10.1128/jb.180.15.3873-3881.1998.

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ABSTRACT The bacterial heat shock response is characterized by the elevated expression of a number of chaperone complexes and proteases, including the DnaK-GrpE-DnaJ and the GroELS chaperone complexes. In order to investigate the importance of the DnaK chaperone complex for growth and heat shock response regulation in Lactococcus lactis, we have constructed two dnaK mutants with C-terminal deletions in dnaK. The minor deletion of 65 amino acids in the dnaKΔ2 mutant resulted in a slight temperature-sensitive phenotype. BK6, containing the larger deletion of 174 amino acids (dnaKΔ1), removing th

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Lebepe, Charity Mekgwa, Pearl Rutendo Matambanadzo, Xolani Henry Makhoba, Ikechukwu Achilonu, Tawanda Zininga, and Addmore Shonhai. "Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone." Biomolecules 10, no. 6 (2020): 856. http://dx.doi.org/10.3390/biom10060856.

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Hsp70 is a conserved molecular chaperone. How Hsp70 exhibits specialized functions across species remains to be understood. Plasmodium falciparum Hsp70-1 (PfHsp70-1) and Escherichia coli DnaK are cytosol localized molecular chaperones that are important for the survival of these two organisms. In the current study, we investigated comparative structure-function features of PfHsp70-1 relative to DnaK and a chimeric protein, KPf, constituted by the ATPase domain of DnaK and the substrate binding domain (SBD) of PfHsp70-1. Recombinant forms of the three Hsp70s exhibited similar secondary and tert

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Lee, Jung Ho, Dongyu Zhang, Christopher Hughes, Yusuke Okuno, Ashok Sekhar, and Silvia Cavagnero. "Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone." Proceedings of the National Academy of Sciences 112, no. 31 (2015): E4206—E4215. http://dx.doi.org/10.1073/pnas.1505173112.

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The molecular chaperone heat shock protein 70 (Hsp70) plays a vital role in cellular processes, including protein folding and assembly, and helps prevent aggregation under physiological and stress-related conditions. Although the structural changes undergone by full-length client proteins upon interaction with DnaK (i.e., Escherichia coli Hsp70) are fundamental to understand chaperone-mediated protein folding, these changes are still largely unexplored. Here, we show that multiple conformations of the SRC homology 3 domain (SH3) client protein interact with the ADP-bound form of the DnaK chape

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Dissertations / Theses on the topic "Molecular chaperone DnaK"

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Simpkins, Sean A. "The DnaK molecular chaperone of Rhizobium leguminosarum." Thesis, University of East Anglia, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.302035.

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Anglès, Frédéric. "Impact of the molecular chaperone HSP70/DnaK on the Escherichia coli central metabolism." Thesis, Toulouse 3, 2015. http://www.theses.fr/2015TOU30126.

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Le réseau de protéines chaperons est hautement conservé dans l'ensemble du vivant. Il régule l'homéostasie des protéines au sein de la cellule en condition de croissance normale ainsi qu'en réponse à des stress environnementaux. Les chaperons membres de la famille HSP70 (Heat Shock Protein 70 kDa), famille particulièrement conservée, agissent tout au long de la biogénèse des protéines et orchestrent une pléthore de processus cellulaires liés au repliement et/ou au remodelage de protéines. Le cycle ATP-dépendant du chaperon HSP70 repose sur une étroite collaboration avec ses partenaires co-chap

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Akhrymuk, Alena [Verfasser]. "Studies on the interaction between the molecular chaperone DnaK and Nucleotide exchange factor GrpE from Thermus thermophilus / Alena Akhrymuk." Dortmund : Universitätsbibliothek Technische Universität Dortmund, 2004. http://d-nb.info/1011532042/34.

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Adell, Moruno Maria. "Caracterización bioquímica y estructural de la chaperona DnaK de Mycoplasma genitalium." Doctoral thesis, Universitat de Barcelona, 2015. http://hdl.handle.net/10803/299789.

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Mycoplasma genitalium es un patógeno humano considerado uno de los organismos autorreplicativos más pequeños que existen. Su genoma fue completamente secuenciado en 1995, y actualmente, se ha convertido en un intenso objeto de estudio porque ha sido descrito como modelo ideal de célula mínima. M. genitalium presenta una morfología celular caracterizada por una extensión de la membrana en uno de los polos de la célula, conocido como Organela Terminal (OT). La OT está involucrada en procesos celulares tales como adhesión, división celular y motilidad con implicaciones directas en patogenicidad y

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Krenek, Sascha, Martin Schlegel, and Thomas U. Berendonk. "Convergent evolution of heat-inducibility during subfunctionalization of the Hsp70 gene family." Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-126934.

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Background: Heat-shock proteins of the 70 kDa family (Hsp70s) are essential chaperones required for key cellular functions. In eukaryotes, four subfamilies can be distinguished according to their function and localisation in different cellular compartments: cytosol, endoplasmic reticulum, mitochondria and chloroplasts. Generally, multiple cytosol-type Hsp70s can be found in metazoans that show either constitutive expression and/or stress-inducibility, arguing for the evolution of different tasks and functions. Information about the hsp70 copy number and diversity in microbial eukaryotes is, ho

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Bruel, Nicolas. "Hsp33 controls elongation factor-tu stability and allows escherichia coli growth in the absence of the major dnak and triggerfactor chaperones." Toulouse 3, 2013. http://thesesups.ups-tlse.fr/2098/.

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Le repliement intracellulaire des protéines nouvellement synthétisées est assisté par des réseaux cellulaires de protéines chaperons. Chez Escherichia coli, la coopération entre les protéines chaperons Trigger Factor (TF) et DnaK est prédominante dans ce processus. En accord avec ceci, la délétion simultanée des gènes codants pour ces deux protéines chaperons conduit à une croissance bactérienne très réduite et à l'accumulation d'un grand nombre de protéines cytoplasmiques sous forme d'agrégats. Au cours de cette étude, nous avons utilisé ces phénotypes afin de mettre en évidence des interacti

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Partensky, Peretz. "Contributions of DNA, histone chaperones and chromatin remodeling enzymes to nucleosome positioning." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3390069.

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Georg, Raphaela de Castro. "Análise da expressão gênica em resposta ao choque térmico e cádmio no fungo aquático Blastocladiella emersonii." Universidade de São Paulo, 2006. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-18042007-125925/.

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Neste trabalho realizamos um programa de seqüenciamento em larga escala de cDNAs obtidos de bibliotecas construídas a partir de mRNA de células de B. emersonii submetidas ao choque térmico e ao estresse por cádmio. Obtivemos 6350 seqüências expressas (ESTs) de alta qualidade, que representam 2326 seqüências únicas putativas (unigenes) do fungo. Destes unigenes putativos, 1282 genes foram classificados em pelo menos uma das categorias do Consórcio Gene Ontology (GO). A análise do transcriptoma parcial de B. emersonii determinado até o momento permitiu a identificação de 78 unigenes codificando

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Ludewig, Michael Hans. "The characterisation of trypanosomal type 1 DnaJ-like proteins." Thesis, Rhodes University, 2010. http://hdl.handle.net/10962/d1015205.

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Trypanosomes are protozoans, of which many are parasitic, and possess complex lifecycles which alternate between mammalian and arthropod hosts. As is the case with most organisms, molecular chaperones and heat shock proteins are encoded within the genomes of these protozoans. These proteins are an integral part of maintaining the structural integrity of proteins during normal and stress conditions. Heat shock protein 40 (Hsp40) is a co-chaperone of heat shock protein 70 (Hsp70) and in some cases can act as a chaperone. These proteins work together to bind non-native polypeptide structures to p

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Ramey, Christopher Joshua. "The role of histone H3/H4 chaperone anti-silencing function1 in maintaining genomic integrity /." Connect to full text via ProQuest. IP filtered, 2006.

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Thesis (Ph.D. in Molecular Biology) -- University of Colorado at Denver and Health Sciences Center, 2006.<br>Typescript. Includes bibliographical references (leaves 119-130). Free to UCDHSC affiliates. Online version available via ProQuest Digital Dissertations;

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Books on the topic "Molecular chaperone DnaK"

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Pierpaoli, Ezra Valerio. Mechanism of action of the DnaK/DnaJ/GrpE molecular chaperone system of escherichia coli. [s.n.], 1997.

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Book chapters on the topic "Molecular chaperone DnaK"

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Zylicz, M. "The Escherichia coli chaperones involved in DNA replication." In Molecular Chaperones. Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-2108-8_3.

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McCauley, Micah J., Joha Joshi, Nicole Becker, et al. "Quantifying ATP-Independent Nucleosome Chaperone Activity with Single-Molecule Methods." In Single Molecule Analysis. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3377-9_2.

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AbstractThe dynamics of histone-DNA interactions govern chromosome organization and regulates the processes of transcription, replication, and repair. Accurate measurements of the energies and the kinetics of DNA binding to component histones of the nucleosome under a variety of conditions are essential to understand these processes at the molecular level. To accomplish this, we employ three specific single-molecule techniques: force disruption (FD) with optical tweezers, confocal imaging (CI) in a combined fluorescence plus optical trap, and survival probability (SP) measurements of disrupted

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Hibino, T., M. Sugino, K. Tsujimura, et al. "Molecular Chaperon DnaK from A Halotolerant Cyanobacterium Aphanothece halopytica." In Photosynthesis: Mechanisms and Effects. Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_688.

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Paro, Renato, Ueli Grossniklaus, Raffaella Santoro, and Anton Wutz. "Chromatin Dynamics." In Introduction to Epigenetics. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-68670-3_2.

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AbstractThe nucleus of a eukaryotic cell is a very busy place. Not only during replication of the DNA, but at any time in the cell cycle specific enzymes need access to genetic information to process reactions such as transcription and DNA repair. Yet, the nucleosomal structure of chromatin is primarily inhibitory to these processes and needs to be resolved in a highly orchestrated manner to allow developmental, organismal, and cell type-specific nuclear activities. This chapter explains how nucleosomes organize and structure the genome by interacting with specific DNA sequences. Variants of c

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Landry, Samuel J., and Lila M. Gierasch. "Recognition of peptides by the E. coli molecular chaperones, GroEL and DnaK." In Peptides. Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_70.

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Knighton, Laura E., and Andrew W. Truman. "Role of the Molecular Chaperones Hsp70 and Hsp90 in the DNA Damage Response." In Heat Shock Proteins. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-03952-3_18.

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ów, A. Wawrzyn, and M. Zyl ícz. "The role of molecular chaperones in DNA replication." In Guidebook to Molecular Chaperones and Protein-Folding Catalysts. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780198599494.003.00188.

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Abstract The role of the DnaK/DnaJ/GrpE molecular chaperones has been described in detail for a few DNA replication systems, namely, A, mini-F, mini-P1 and oriC plasmid DNA replication. Only in the case of the A DNA replication system has it been shown that the DnaK/DnaJ/GrpE chaperone machine is directly involved in the initiation process. In all other cases, the DnaK/DnaJ/GrpE chaperones activate the initiation proteins but do not participate during the final DNA replication initiation event. Recently, studies on the bacteriophage Mu DNA replication have suggested that this system could be a

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Bukau, B. "The heat shock response in Escherichia coli." In Guidebook to Molecular Chaperones and Protein-Folding Catalysts. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780198599494.003.00194.

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Abstract The conserved heat shock (stress) response allows cells to adapt to environmental and metabolic changes and to survive stress conditions (Morimoto et al., 1994). It is induced by a large variety of stress conditions including physicochemical factors such as heat shock, metabolically harmful substances and complex metabolic processes. In Escherichia coli, the heat shock response to temperature upshift from 30 to 42°C consists of the rapid, up to 20-fold, induction of synthesis of more than 20 heat shock proteins (HSPs), followed by an adaptation period where the rate of HSP synthesis d

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"THE DnaK CHAPERONE SYSTEM: MECHANISM AND COMPARISON WITH OTHER HSP70 SYSTEMS." In Molecular Chaperones and Folding Catalysts. CRC Press, 1999. http://dx.doi.org/10.1201/9781482283440-37.

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Smith, D. F. "The pathway of assembly of the progesterone receptor." In Guidebook to Molecular Chaperones and Protein-Folding Catalysts. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780198599494.003.00193.

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Abstract The PR assembly pathway minimally involves the following chaperone components: Hsp90, Hsc70, Hip, Hop (p60), p23, FKBP52, FKBP51, and Cyp40 (Smith etal., 1995 and references therein; also see the individual entries in this volume for these and other chaperones mentioned in this review). There is also genetic evidence from steroid receptor expression in yeast cells that Ydj1, a cytosolic DnaJ homolog, is required for proper function of steroid receptors (Caplan et al., 1995; Kimura et al., 1995).

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Reports on the topic "Molecular chaperone DnaK"

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Galili, Gad, and Alan Bennett. Role of Molecular Chaperone in Wheat Storage Protein Assembly. United States Department of Agriculture, 1995. http://dx.doi.org/10.32747/1995.7604926.bard.

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Following sequestration into the ER, wheat gliadins assemble into complexes that initiate the formation of protein bodies. In the present work we have characterized the DNA sequence and regulation of expression of a plant BiP and also studied its interaction with wheat storage proteins as well as its role in the maturation of these storage proteins. In the Israeli lab, immunoprecipitation studies were made using anti BiP and anti storage proteins sera, both in wheat and in transgenic tobacco plants expressing a wheat gliadin storage proteins. In both cases, we could show that BiP interacts wit

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Tzfira, Tzvi, Michael Elbaum, and Sharon Wolf. DNA transfer by Agrobacterium: a cooperative interaction of ssDNA, virulence proteins, and plant host factors. United States Department of Agriculture, 2005. http://dx.doi.org/10.32747/2005.7695881.bard.

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Agrobacteriumtumefaciensmediates genetic transformation of plants. The possibility of exchanging the natural genes for other DNA has led to Agrobacterium’s emergence as the primary vector for genetic modification of plants. The similarity among eukaryotic mechanisms of nuclear import also suggests use of its active elements as media for non-viral genetic therapy in animals. These considerations motivate the present study of the process that carries DNA of bacterial origin into the host nucleus. The infective pathway of Agrobacterium involves excision of a single-stranded DNA molecule (T-strand

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Savova, Gergana, Katya Stankova, Nevena Aneva, and Rayna Boteva. Geldanamycin, Natural Benzoquinone and Inhibitor of the Molecular Chaperone Hsp90, Accelerates the Repair of DNA Doublestrand Breaks in Human Blood Cells. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, 2021. http://dx.doi.org/10.7546/crabs.2021.05.08.

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