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1
Isolation and characterization of a DnaJ-like protein in rats: the C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like protein.大鼠中一种类DnaJ蛋白的分离与鉴定：热休克同源蛋白70（hsc70）的C末端10 kDa结构域对于类DnaJ蛋白刺激hsc70的ATP水解活性并非必需。
Protein Sci. 1998 May;7(5):1186-94. doi: 10.1002/pro.5560070513.
2
Involvement of the 10-kDa C-terminal fragment of hsc70 in complexing with unfolded protein.热休克蛋白70（hsc70）的10 kDa C末端片段参与与未折叠蛋白的复合。
Arch Biochem Biophys. 1996 Aug 1;332(1):163-9. doi: 10.1006/abbi.1996.0328.
3
A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40.克氏锥虫热休克蛋白40能够刺激热休克蛋白70的三磷酸腺苷水解活性，并且可以替代酵母热休克蛋白40。
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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.DnaJ与DnaK之间等位基因特异性遗传相互作用的结构与能量学：Hsp40/DnaJ的J结构域中核磁共振化学位移扰动与对Hsp70/DnaK的ATP酶结构域结合亲和力的相关性
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5
Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone.肽与牛70 kDa热休克同源蛋白（一种分子伴侣）结合的动力学
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The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70.热休克蛋白40（Hsp40）的J结构域将ATP水解与热休克蛋白70（Hsp70）中的底物捕获偶联起来。
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Upregulation of the cochaperone Mdg1 in endothelial cells is induced by stress and during in vitro angiogenesis.伴侣蛋白Mdg1在内皮细胞中的上调是由应激和体外血管生成过程诱导的。
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Effect of yeast and human DnaJ homologs on clathrin uncoating by 70 kilodalton heat shock protein.酵母和人类DnaJ同源物对70千道尔顿热休克蛋白介导的网格蛋白去包被的影响。
Biochemistry. 1997 Apr 8;36(14):4067-73. doi: 10.1021/bi9625307.
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Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b.人源类DnaJ蛋白HSJ1a和HSJ1b对70-kDa热休克蛋白ATP酶活性及底物结合的调控
Eur J Biochem. 1994 Nov 15;226(1):99-107. doi: 10.1111/j.1432-1033.1994.tb20030.x.
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Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles.网格蛋白包被小泡催化去包被所需的发动蛋白辅助蛋白功能片段的结构。
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1
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Cloning and molecular characterization of heat shock cognate 70 from tiger shrimp (Penaeus monodon).斑节对虾热休克同源蛋白70的克隆与分子特征分析
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Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s.与其他热休克蛋白70相比，核糖体相关分子伴侣Ssb的功能特性存在差异。
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4
Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins.热休克同源蛋白70（hsc70）C末端功能基团的不同组合被用于与不同的含四肽重复序列蛋白相互作用。
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Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature.哺乳动物热休克蛋白40/DNAJ同源物：新cDNA的克隆及其分类和命名建议。
Cell Stress Chaperones. 2000 Apr;5(2):98-112. doi: 10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2.
6
Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1.小鼠BiP/GRP78与DnaJ同源物MTJ1的相互作用。
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本文引用的文献

1
The amino-terminal transforming region of simian virus 40 large T and small t antigens functions as a J domain.猴病毒40大T抗原和小t抗原的氨基末端转化区作为一个J结构域发挥作用。
Mol Cell Biol. 1997 Aug;17(8):4761-73. doi: 10.1128/MCB.17.8.4761.
2
The cysteine string secretory vesicle protein activates Hsc70 ATPase.半胱氨酸串珠分泌囊泡蛋白激活Hsc70 ATP酶。
J Biol Chem. 1996 Oct 18;271(42):25989-93. doi: 10.1074/jbc.271.42.25989.
3
Involvement of the 10-kDa C-terminal fragment of hsc70 in complexing with unfolded protein.热休克蛋白70（hsc70）的10 kDa C末端片段参与与未折叠蛋白的复合。
Arch Biochem Biophys. 1996 Aug 1;332(1):163-9. doi: 10.1006/abbi.1996.0328.
4
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.大肠杆菌DnaJ伴侣蛋白J结构域和富含甘氨酸/苯丙氨酸区域的核磁共振结构
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Identification of elements of the peptide binding site of DnaK by peptide cross-linking.
J Biol Chem. 1996 Aug 16;271(33):19668-74.
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Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40.哺乳动物DnaJ同源物Hsp40对热休克蛋白70反应循环的调控
J Biol Chem. 1996 Aug 9;271(32):19617-24. doi: 10.1074/jbc.271.32.19617.
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Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone.DnaJ分子伴侣锌指区域的结构-功能分析
J Biol Chem. 1996 Jun 21;271(25):14840-8. doi: 10.1074/jbc.271.25.14840.
8
Structural analysis of substrate binding by the molecular chaperone DnaK.分子伴侣DnaK对底物结合的结构分析
Science. 1996 Jun 14;272(5268):1606-14. doi: 10.1126/science.272.5268.1606.
9
A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.分子伴侣DnaJ的一个锌指样结构域参与与变性蛋白质底物的结合。
EMBO J. 1996 Jan 15;15(2):408-17.
10
Rat kidney glutathione S-transferase 1 subunits have C-terminal truncations.大鼠肾脏谷胱甘肽S-转移酶1亚基具有C端截短。
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大鼠中一种类DnaJ蛋白的分离与鉴定：热休克同源蛋白70（hsc70）的C末端10 kDa结构域对于类DnaJ蛋白刺激hsc70的ATP水解活性并非必需。

Isolation and characterization of a DnaJ-like protein in rats: the C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like protein.

作者信息

Leng C H, Brodsky J L, Wang C

机构信息

Institute of Molecular Biology, Academia Sinica, National Defense Medical Center, Taipei, Taiwan.

出版信息

Protein Sci. 1998 May;7(5):1186-94. doi: 10.1002/pro.5560070513.

DOI:10.1002/pro.5560070513
PMID:9605323
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2143995/
Abstract

A DnaJ-like protein, RDJ1, was isolated from a rat brain cDNA library. The protein is predicted to have 397 amino acid residues and shares 99% identity to that of HDJ2, a human DnaJ-like protein. RDJ1 was also shown to rescue the temperature-sensitive lethality of a strain containing a mutated cytosolic DnaJ in yeast, ydj1-151. Fragments containing the J-domain of RDJ1 either with or without the G/F motif were expressed in Escherichia coli. The purified proteins stimulated the ATPase activity of hsc70 and of the 60-kDa N-terminal fragment of hsc70. These results imply that RDJ1 can interact with the N-terminal 60-kDa fragment of hsc70 to activate ATP hydrolysis by hsc70.

摘要

一种类DnaJ蛋白RDJ1是从大鼠脑cDNA文库中分离得到的。该蛋白预计含有397个氨基酸残基，与人类类DnaJ蛋白HDJ2的氨基酸序列一致性达99%。此外，RDJ1能够拯救酵母中含有突变胞质DnaJ的菌株ydj1 - 151的温度敏感性致死效应。含有RDJ1的J结构域且带有或不带有G/F基序的片段在大肠杆菌中表达。纯化后的蛋白刺激了hsc70以及hsc70 60 kDa N端片段的ATP酶活性。这些结果表明，RDJ1能够与hsc70的N端60 kDa片段相互作用，从而激活hsc70的ATP水解。