The Roles of the Two Zinc Binding Sites in DnaJ

Linke, Katrin; Wolfram, Tobias; Bussemer, Johanna; Jakob, Ursula

doi:10.1074/jbc.m307491200

Cited by 98 publications

(100 citation statements)

References 41 publications

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“…2B) is important for interaction of DnaJ with another chaperone protein, DnaK (44,45). Substitution of any cysteine residue by serine in this domain reduced DnaK-dependent chaperone activity (44). Similar results were obtained for Ydj1, a close homologue of DnaJ in yeast (46).…”

Section: Resultssupporting

confidence: 72%

“…The second zinc-binding domain (Zn2 in Fig. 2B) is important for interaction of DnaJ with another chaperone protein, DnaK (44,45). Substitution of any cysteine residue by serine in this domain reduced DnaK-dependent chaperone activity (44).…”

Section: Resultsmentioning

confidence: 99%

“…2B) interacts with unfolded proteins to prevent their aggregation (41). Indeed, substitution of any cysteine residue by serine in this domain resulted in mutant proteins with reduced ability to bind to denatured proteins (44). The second zinc-binding domain (Zn2 in Fig.…”

Section: Resultsmentioning

confidence: 99%

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Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction

Shevtsov

Chen

Gollnick

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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In Bacillus subtilis the anti-TRAP protein (AT) is produced in response to the accumulation of uncharged tRNA Trp . AT regulates expression of genes involved in tryptophan biosynthesis and transport by binding to the tryptophan-activated trp RNA-binding attenuation protein (TRAP) and preventing its interaction with several mRNAs. Here, we report the x-ray structure of AT at 2.8 Å resolution, showing that the protein subunits assemble into tight trimers. Four such trimers are further associated into a 12-subunit particle in which individual trimers are related by twofold and threefold symmetry axes. Twelve DnaJ-like, cysteine-rich zincbinding domains form spikes on the surface of the dodecamer. Available data suggest several possible ways for AT to interact with the 11-subunit TRAP. Interaction between the two symmetrymismatching molecules could be assisted by the flexible nature of AT zinc-binding domains.DnaJ ͉ trp RNA-binding attenuation protein ͉ tryptophan biosynthesis ͉ protein-protein interactions

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Section: Resultssupporting

confidence: 72%

Section: Resultsmentioning

confidence: 99%

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Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction

Shevtsov

Chen

Gollnick

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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“…(17). It has been reported that zinc finger 1 is necessary for the autonomous chaperone activity in cooperation with the C-terminal domain (5,7,13), and zinc finger 2 together with the J domain are absolutely essential for the interaction with DnaK (13). Thus, we localized the zinc finger domain in such a way to make zinc finger 1 toward C-terminal domain and the zinc finger 2 close to the J domain, for fitting the different functions of the two zinc fingers.…”

Section: Saxs Parameters-as Shown Inmentioning

confidence: 99%

“…In addition to the DnaK-dependent co-chaperone activity described above, DnaJ also exerts autonomous DnaK-independent chaperone activity (9,12,13), which is characterized by its ability to bind with unfolded proteins and prevent them from irreversible aggregation (10,11). Moreover, DnaJ has been found to have thiol-disulfide oxidoreductase activity but little, if any, isomerase activity (14).…”

mentioning

confidence: 99%

The C-terminal (331–376) Sequence of Escherichia coli DnaJ Is Essential for Dimerization and Chaperone Activity

Shi

Hong

Wang

2005

Journal of Biological Chemistry

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DnaJ, an Escherichia coli Hsp40 protein composed of 376 amino acid residues, is a chaperone with thioldisulfide oxidoreductase activity. We present here for the first time a small angle x-ray scattering study of intact DnaJ and a truncated version, DnaJ (1-330), in solution. The molecular weight of DnaJ and DnaJ (1-330) determined by both small angle x-ray scattering and size-exclusion chromatography provide direct evidence that DnaJ is a homodimer and DnaJ (1-330) is a monomer. The restored models show that DnaJ is a distorted -shaped dimeric molecule with the C terminus of each subunit forming the central part of the , whereas DnaJ (1-330) exists as a monomer. This indicates that the deletion of the C-terminal 46 residues of DnaJ impairs the association sites, although it does not cause significant conformational changes. Biochemical studies reveal that DnaJ (1-330), while fully retaining its thiol-disulfide oxidoreductase activity, is structurally less stable, and its peptide binding capacity is severely impaired relative to that of the intact molecule. Together, our results reveal that the C-terminal (331-376) residues are directly involved in dimerization, and the dimeric structure of DnaJ is necessary for its chaperone activity but not required for the thiol-disulfide oxidoreductase activity.Hsp40 proteins collaborate specifically with Hsp70 proteins and some other factors to participate in a wide range of cellular processes essential to cell survival, such as assisting the folding, assembly, disassembly, and translocation of newly synthesized proteins, by suppressing aggregation or mediating degradation of misfolded proteins (1, 2). The Hsp40 family proteins are divided into three subtypes (3) (see Scheme 1). They all contain a J domain responsible for binding to the ATPase domain and stimulating the ATPase activity of Hsp70. Type I Hsp40 proteins, such as Escherichia coli DnaJ, yeast Yjd1, and human Hdj-2, have a Gly/Phe-rich region, which has been suggested to assist J domain interactions with Hsp70 (4). The Gly/Phe-rich region is followed by a conserved cysteine-rich region forming a zinc finger domain and a poorly conserved C-terminal domain. The peptide binding site(s) has been found to locate within these two domains (5-7). Type II Hsp40 proteins, such as yeast Sis1 and mammalian Hdj-1, also contain the J, a Gly/Phe-rich region, and C-terminal domains but without the zinc finger domain (8, 9). Both type I and type II Hsp40 proteins act as molecular chaperones to bind and deliver nonnative proteins to Hsp70 (7, 8, 10), but they are not functionally equivalent (11). Type III Hsp40 proteins, such as yeast YJL162c and virus T antigen, contain only the J domain, and they do not function as molecular chaperones (3).In addition to the DnaK-dependent co-chaperone activity described above, DnaJ also exerts autonomous DnaK-independent chaperone activity (9, 12, 13), which is characterized by its ability to bind with unfolded proteins and prevent them from irreversible aggregation (10, 11). Moreover, DnaJ has ...

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Regulation of Hsp70 Chaperones by Co‐chaperones

Mayer¹,

Bukau²

2005

Protein Folding Handbook

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The Roles of the Two Zinc Binding Sites in DnaJ

Cited by 98 publications

References 41 publications

Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction

Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction

The C-terminal (331–376) Sequence of Escherichia coli DnaJ Is Essential for Dimerization and Chaperone Activity

Regulation of Hsp70 Chaperones by Co‐chaperones

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