The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.
The Escherichia coli Hsp40 DnaJ uses its J-domain (Jd) to couple ATP hydrolysis and client protein capture in Hsp70 DnaK. Fusion of the Jd to peptide p5 (as in Jdp5) dramatically increases the apparent affinity of the p5 moiety for DnaK in the presence of ATP, and Jdp5 stimulates ATP hydrolysis in DnaK by several orders of magnitude. NMR experiments with [(15)N]Jdp5 demonstrated that the peptide tethers the Jd to the ATPase domain. Thus, ATP hydrolysis and client protein binding in DnaK are coupled principally through the association of the client with DnaJ. Overexpression of a recombinant Jd was specifically toxic to cells that simultaneously expressed DnaK. No toxicity was observed when overexpressing Jdp5 or mutant Jd or when co-overexpressing the Jd and the nucleotide exchange factor GrpE. The results suggest that the Jd shifts DnaK to a client-bound form by stimulating the DnaK ATPase but only when the Jd is brought to DnaK by a client-Hsp40 complex.
Horne
B Erin
BE
Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112, USA.
Li
Tingfeng
T
Genevaux
Pierre
P
Georgopoulos
Costa
C
Landry
Samuel J
SJ
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D018833:Chaperonins / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry; D050956:HSP40 Heat-Shock Proteins / Q000737:chemistry*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry*; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D018832:Molecular Chaperones; D009154:Mutation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry
D029968:Escherichia coli Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D011994:Recombinant Proteins; D000251:Adenosine Triphosphatases; D018833:Chaperonins; C063842:dnaK protein, E coli
Cell Stress Chaperones. 1998 Mar;3(1):28-36
9585179
Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):9269-76
10430932
Biochemistry. 2002 Oct 8;41(40):12224-35
12356325
Mol Microbiol. 2007 Nov;66(4):840-57
17919282
J Biol Chem. 2003 May 23;278(21):19038-43
12654915
Nature. 1990 Aug 16;346(6285):623-8
2143562
Annu Rev Biochem. 2001;70:603-47
11395418
Biochemistry. 1998 Jan 13;37(2):596-607
9425082
J Biol Chem. 2001 Jul 20;276(29):27231-6
11352903
Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):3679-84
9108037
J Bacteriol. 2006 May;188(10):3494-7
16672603
J Bacteriol. 1989 May;171(5):2748-55
2651417
J Neurosci. 1999 Dec 1;19(23):10338-47
10575031
J Bacteriol. 1995 Jul;177(14):4121-30
7608087
J Mol Biol. 1998 Jun 19;279(4):833-40
9642064
Biochemistry. 1998 Nov 24;37(47):16749-56
9843445
Nat Struct Biol. 2000 Jul;7(7):586-93
10876246
Proc Natl Acad Sci U S A. 2008 Jan 29;105(4):1164-9
18203820
Mol Cell. 2005 Nov 23;20(4):513-24
16307916
Science. 1996 Jun 14;272(5268):1606-14
8658133
Proc Natl Acad Sci U S A. 1998 May 26;95(11):6108-13
9600925
Genetics. 2002 Nov;162(3):1045-53
12454054
J Biol Chem. 2006 May 5;281(18):12436-44
16533811
J Bacteriol. 1989 Nov;171(11):6030-8
2681151
EMBO J. 2001 Jan 15;20(1-2):262-71
11226176
Biochemistry. 2003 May 6;42(17):4937-44
12718535
Mol Cell. 1998 Nov;2(5):593-603
9844632
Cell. 2007 Oct 5;131(1):106-20
17923091
EMBO Rep. 2004 Feb;5(2):195-200
14726952
J Biol Chem. 2006 Jan 20;281(3):1605-11
16275641
Mol Cell. 2007 Apr 13;26(1):27-39
17434124
Biochemistry. 1999 Mar 30;38(13):4165-76
10194333
J Mol Biol. 1999 Jun 18;289(4):1131-44
10369787
J Bacteriol. 2001 Oct;183(19):5482-90
11544208
J Biol Chem. 1996 May 10;271(19):11236-46
8626673
Biochemistry. 1997 Mar 25;36(12):3417-22
9131990
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15223-8
9860950
Proc Natl Acad Sci U S A. 1999 May 11;96(10):5452-7
10318904
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15229-34
9860951
Nat Cell Biol. 2001 Feb;3(2):215-9
11175756
Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2874-8
1826368