Histidine 89 is an essential residue for Hsp70 in the phosphate transfer reaction

Cell Stress and Chaperones

Volumn 11, Issue 2, 2006, Pages 148-153

  Lu, Yuanming ^a   Hu, Qian ^a   Yang, Cuixia ^a   Gao, Feng ^a  

^a SHANGHAI JIAO TONG UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTIDINE DIPHOSPHATE; GLYCINE; HEAT SHOCK PROTEIN 70; HISTIDINE; PHOSPHATE; SERINE;

AMINO ACID SUBSTITUTION; CONFERENCE PAPER; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE MUTATION; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; REACTION ANALYSIS; RESIDUE ANALYSIS; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; BINDING SITES; CYTIDINE DIPHOSPHATE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCINE; HISTIDINE; HSP70 HEAT-SHOCK PROTEINS; HUMANS; HYDROLYSIS; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; NUCLEOSIDE-DIPHOSPHATE KINASE; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; SERINE;

EID: 33745454983     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1379/CSC-152R.1     Document Type: Conference Paper

References (23)

1. Amir-Shapira D, Leustek T, Dalie B, Weissbach H, Brot N. 1990. Hsp70 proteins, similar to Escherichia coli DnaK in chloroplasts and mitochondria of Euglena gracilis. Proc Natl Acad Sci U S A 87: 1749-1752.
2. Becker J, Craig EA. 1994. Heat shock proteins as molecular chaperones. Eur J Biochem 219: 11-23.
3. Braell WA, Schlossman DM, Schmid SL, Rothman JE. 1984. Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase. J Cell Biol 99: 734-741.
4. Bukau B, Horwich AL. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
5. Cegielska A, Georgopoulos C. 1989. Functional domains of the Escherichia coli DnaK heat shock protein as revealed by mutational analysis. J Biol Chem 264: 21122-21130.
6. Flynn GC, Chappell TG, Rothman JE. 1989. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245: 385-390.
7. Frejie JM, Blay P, MacdDonald NJ, Manrow RE, Steeg PS. 1997. Site-directed mutation of Nm23-H1. J Biol Chem 272: 5525-5532.
8. Gaut JR, Hendershot LM. 1993. The immunoglobulin binding protein in vitro autophophorylation site maps to a threonine within the ATP binding cleft but is not a detectable site of in vivo phosphorylation. J Biol Chem 268: 12691-12696.
9. Hendershot LM, Ting J, Lee AS. 1988. Identity of the immunoglobulin heavy chain binding protein with the 78,000 dalton glucose regulated protein and the role of post-translational modifications in its binding function. Mol Cell Biol 24: 4250-4256.
10. Hiromura M, Yano M, Mori H, Inoue M, Kido H. 1998. Intrinsic ADP-ATP exchange activity is a novel function of the molecular chaperone Hsp70. J Biol Chem 273: 5435-5438.
11. Hunter T, Sefton BM. 1980. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci U S A 77: 1311-1315.
12. Leung SM, Hightower LE. 1997. A 16-kDa protein functions as a new regulatory protein for Hsc70 molecular chaperone and is identified as a member of the Nm23/nucleoside diphosphate kinase family. J Biol Chem 272: 2607-2614.
13. Leustek T, Dalie B, Amir-Shapira D, Brot N, Weissbach H. 1989. A member of the Hsp70 family is localized in mitochondria and resembles Escherichia coli DnaK. Proc Natl Acad Sci U S A 86: 7805-7808.
14. Leustek T, Toledo H, Brot N, Weissbach H. 1991. Calcium-dependent phosphorylation of the glucose regulated protein, Grp78. Arch Biochem Biophys 289: 256-261.
15. Loomis WF, Wheeler S, Schmidt A. 1982. Phosphorylation of the major heat shock protein of Dictyostelium discoideum. Mol Cell Biol 2: 484-489.
16. McCarty JS, Walker GC. 1991. DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc Nat Acad Sci U S A 88: 9513-9517.
17. O'Brien MC, Flaherty KM, McKay DB. 1996. Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis. J Biol Chem 271: 15874-15878.
18. O'Brien MC, McKay DB. 1993. Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis. J Biol Chem 268: 24323-24329.
19. Rieul C, Cortay J, Bleicher F, Cozzone AJ. 1987. Effect of bacteriophage M13 infection on phosphorylation of DnaK protein and other Escherichia coli proteins. Eur J Biochem 168: 621-627.
20. Sriram M, Osipiuk J, Freeman BC, Morimoto RI, Joachimiak A. 1997. Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain. Structure 15: 403-414.
21. Wei YF, Matthews HR. 1991. Identification of phosphohistidine in proteins and purification of protein histidine kinases. Methods Enzymol 200: 388-414.
22. 2+ ionophore regulated. J Biol Chem 258: 7102-7111.
23. Yano M, Mori S, Kido H. 1999. Intrinsic nucleoside diphosphate kinase-like activity is a novel function of the 20 S proteasome. J Biol Chem 274: 34375-34382.