Mechanisms for regulation of Hsp70 function by Hsp40

Abstract The Hsp70 family members play an essential role in cellular protein metabolism by acting as polypeptide-binding and release factors that interact with nonnative regions of proteins at different stages of their life cycles. Hsp40 cochaperone proteins regulate complex formation between Hsp70 and client proteins. Herein, literature is reviewed that describes the mechanisms by which Hsp40 proteins interact with Hsp70 to specify its cellular functions.

[1]  Bernd Bukau,et al.  Its substrate specificity characterizes the DnaJ co‐chaperone as a scanning factor for the DnaK chaperone , 2001, The EMBO journal.

[2]  C. Georgopoulos,et al.  The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication. , 1994, The Journal of biological chemistry.

[3]  M. Cheetham,et al.  Domain Requirements of DnaJ-like (Hsp40) Molecular Chaperones in the Activation of a Steroid Hormone Receptor* , 1999, The Journal of Biological Chemistry.

[4]  D. Cyr,et al.  Purification, crystallization and preliminary X-ray crystallographic studies of S. cerevisiae Hsp40 Sis1. , 1999, Acta crystallographica. Section D, Biological crystallography.

[5]  Craig M. Ogata,et al.  Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK , 1996, Science.

[6]  William J. Welch,et al.  ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysis , 1993, Nature.

[7]  R. Schekman,et al.  A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome , 1993, The Journal of cell biology.

[8]  Judith Frydman,et al.  Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones , 1994, Nature.

[9]  J Kuriyan,et al.  Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. , 1997, Science.

[10]  C. Georgopoulos,et al.  Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[11]  D. Cyr,et al.  The Hdj‐2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis , 1999, The EMBO journal.

[12]  P. Casey,et al.  Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae. , 1992, The Journal of biological chemistry.

[13]  C. Gross,et al.  Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[14]  M. Cheetham,et al.  Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. , 1998, Cell stress & chaperones.

[15]  D. Cyr,et al.  Protein Folding Activity of Hsp70 Is Modified Differentially by the Hsp40 Co-chaperones Sis1 and Ydj1* , 1998, The Journal of Biological Chemistry.

[16]  F. Hartl,et al.  The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[17]  E. Eisenberg,et al.  Role of auxilin in uncoating clathrin-coated vesicles , 1995, Nature.

[18]  M. Douglas,et al.  A Conserved HPD Sequence of the J-domain Is Necessary for YDJ1 Stimulation of Hsp70 ATPase Activity at a Site Distinct from Substrate Binding (*) , 1996, The Journal of Biological Chemistry.

[19]  E. Craig,et al.  The Glycine-Phenylalanine-Rich Region Determines the Specificity of the Yeast Hsp40 Sis1 , 1999, Molecular and Cellular Biology.

[20]  Timothy B. Stockwell,et al.  The Sequence of the Human Genome , 2001, Science.

[21]  T. R. Broker,et al.  Human Hsp70 and Hsp40 Chaperone Proteins Facilitate Human Papillomavirus-11 E1 Protein Binding to the Origin and Stimulate Cell-free DNA Replication* , 1998, The Journal of Biological Chemistry.

[22]  E. Wanker,et al.  Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[23]  P E Wright,et al.  Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. , 2000, Journal of molecular biology.

[24]  W. Neupert,et al.  The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. , 1994, Science.

[25]  D. Cyr.  Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation. , 1995, FEBS letters.

[26]  E. Craig,et al.  The Yeast hsp70 Homologue Ssa Is Required for Translation and Interacts with Sis1 and Pab1 on Translating Ribosomes* , 2001, The Journal of Biological Chemistry.

[27]  C. Sander,et al.  The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. , 1994, The EMBO journal.

[28]  K. Arndt,et al.  The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation , 1993, Cell.

[29]  P. Christen,et al.  Mechanism of the Targeting Action of DnaJ in the DnaK Molecular Chaperone System* , 2003, Journal of Biological Chemistry.

[30]  D. Cyr,et al.  The Conserved Carboxyl Terminus and Zinc Finger-like Domain of the Co-chaperone Ydj1 Assist Hsp70 in Protein Folding* , 1998, The Journal of Biological Chemistry.

[31]  J. Hoskins,et al.  Interaction of the DnaK and DnaJ Chaperone System with a Native Substrate, P1 RepA* , 2002, The Journal of Biological Chemistry.

[32]  J. Hoskins,et al.  Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[33]  D. Cyr,et al.  YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism , 1992, Cell.

[34]  Y Q Qian,et al.  Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. , 1996, Journal of molecular biology.

[35]  A. Caplan,et al.  Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein , 1991, The Journal of cell biology.

[36]  Holger Sondermann,et al.  Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors , 2001, Science.

[37]  L. Hendershot,et al.  Identification and Characterization of a Novel Endoplasmic Reticulum (ER) DnaJ Homologue, Which Stimulates ATPase Activity of BiP in Vitro and Is Induced by ER Stress* , 2002, The Journal of Biological Chemistry.

[38]  D. Cyr,et al.  Regulation of Hsp70 function by a eukaryotic DnaJ homolog. , 1992, The Journal of biological chemistry.

[39]  Soojin Lee,et al.  Identification of Essential Residues in the Type II Hsp40 Sis1 That Function in Polypeptide Binding* , 2002, The Journal of Biological Chemistry.

[40]  Douglas M. Cry,et al.  Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation , 1995 .

[41]  F. Hartl,et al.  Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding , 1992, Nature.

[42]  T. Langer,et al.  DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. , 1994, Trends in biochemical sciences.

[43]  S. Landry.  Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK. , 2003, Biochemistry.

[44]  E. Craig,et al.  Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+]. , 2003, Molecular biology of the cell.

[45]  I. Yahara,et al.  Heat-induced Chaperone Activity of HSP90 (*) , 1996, The Journal of Biological Chemistry.

[46]  C. Georgopoulos,et al.  Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication , 1978, Molecular and General Genetics MGG.

[47]  J. Prestegard,et al.  1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78). , 1995, Biochemistry.

[48]  D. Cyr,et al.  Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue YDJ1. , 1994, The Journal of biological chemistry.

[49]  K. Flaherty,et al.  Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein , 1990, Nature.

[50]  F. Hartl,et al.  Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein , 2002, Science.

[51]  M. Mayer,et al.  Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy. , 1999, Journal of molecular biology.

[52]  C. Georgopoulos,et al.  Structure-Function Analysis of the Zinc Finger Region of the DnaJ Molecular Chaperone* , 1996, The Journal of Biological Chemistry.

[53]  F. Hartl,et al.  A zinc finger‐like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. , 1996, The EMBO journal.

[54]  S. Landry,et al.  Role of the J-domain in the cooperation of Hsp40 with Hsp70. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[55]  S. Lindquist,et al.  The role of Sis1 in the maintenance of the [RNQ+] prion , 2001, The EMBO journal.

[56]  W. Zhang,et al.  Mutations in the Yeast Hsp40 Chaperone Protein Ydj1 Cause Defects in Axl1 Biogenesis and Pro-a-factor Processing* , 1999, The Journal of Biological Chemistry.

[57]  W. Neupert,et al.  Roles for hsp70 in protein translocation across membranes of organelles. , 1996, EXS.

[58]  L. Gierasch,et al.  Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling. , 1999, Journal of molecular biology.

[59]  F. Hartl,et al.  Regulation of the Heat-shock Protein 70 Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40* , 1996, The Journal of Biological Chemistry.

[60]  C. Georgopoulos,et al.  The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[61]  D. Cyr,et al.  The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. , 2000, Structure.

[62]  Walter E. Gall,et al.  The auxilin-like phosphoprotein Swa2p is required for clathrin function in yeast , 2000, Current Biology.

[63]  Bernd Bukau,et al.  The Hsp70 and Hsp60 Chaperone Machines , 1998, Cell.

[64]  A. Goldberg,et al.  The molecular chaperone Ydj1 is required for the p34CDC28-dependent phosphorylation of the cyclin Cln3 that signals its degradation , 1996, Molecular and cellular biology.

[65]  P. Christen,et al.  d-Peptides as Inhibitors of the DnaK/DnaJ/GrpE Chaperone System* , 2003, Journal of Biological Chemistry.

[66]  F. Boschelli,et al.  The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast. , 1996, Molecular biology of the cell.

[67]  D. Cyr,et al.  Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins. , 1993, Molecular biology of the cell.

[68]  K. Arndt,et al.  Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins , 1991, The Journal of cell biology.

[69]  R. Morimoto,et al.  The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj‐1 have distinct roles in recognition of a non‐native protein and protein refolding. , 1996, The EMBO journal.