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. 1994 Dec 6;91(25):12120–12124. doi: 10.1073/pnas.91.25.12120

Similarity of nucleotide interactions of BiP and GTP-binding proteins.

N Brot 1, B Redfield 1, N H Qiu 1, G J Chen 1, V Vidal 1, A Carlino 1, H Weissbach 1
PMCID: PMC45388  PMID: 7527551

Abstract

BiP is a member of the Hsp70 heat shock protein family found in the lumen of the endoplasmic reticulum, that binds to a variety of proteins destined to be secreted. Substance P (SP) has been used as a model peptide to study the interaction of BiP with protein substrates. SP stimulates BiP ATPase activity and forms a stable complex with BiP that is dissociated in the presence of levels of ATP > 50 microM. At lower concentrations of ATP, the SP remains bound to BiP, and the results are consistent with the view that a BiP-ATP complex is initially formed that reacts with SP to form a ternary complex, SP-BiP-ATP. Hydrolysis of ATP in this complex yields a SP-BiP-ADP complex. An exchange of ATP with ADP bound to BiP has also been demonstrated, and the results suggest that the interactions of BiP with ATP resemble those seen with GTP-binding proteins and GTP.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Allende J. E., Seeds N. W., Conway T. W., Weissbach H. Guanosine triphosphate interaction with an amino acid polymerization factor from E. coli. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1566–1573. doi: 10.1073/pnas.58.4.1566. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Beckmann R. P., Mizzen L. E., Welch W. J. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science. 1990 May 18;248(4957):850–854. doi: 10.1126/science.2188360. [DOI] [PubMed] [Google Scholar]
  3. Blond-Elguindi S., Fourie A. M., Sambrook J. F., Gething M. J. Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers. J Biol Chem. 1993 Jun 15;268(17):12730–12735. [PubMed] [Google Scholar]
  4. Blount P., Merlie J. P. BIP associates with newly synthesized subunits of the mouse muscle nicotinic receptor. J Cell Biol. 1991 Jun;113(5):1125–1132. doi: 10.1083/jcb.113.5.1125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bole D. G., Hendershot L. M., Kearney J. F. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J Cell Biol. 1986 May;102(5):1558–1566. doi: 10.1083/jcb.102.5.1558. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. CONWAY T. W., LIPMANN F. CHARACTERIZATION OF A RIBOSOME-LINKED GUANOSINE TRIPHOSPHATASE IN ESCHERICHIA COLI EXTRACTS. Proc Natl Acad Sci U S A. 1964 Dec;52:1462–1469. doi: 10.1073/pnas.52.6.1462. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Carlino A., Toledo H., Skaleris D., DeLisio R., Weissbach H., Brot N. Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: multiple species and disaggregation. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2081–2085. doi: 10.1073/pnas.89.6.2081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dorner A. J., Bole D. G., Kaufman R. J. The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins. J Cell Biol. 1987 Dec;105(6 Pt 1):2665–2674. doi: 10.1083/jcb.105.6.2665. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Flynn G. C., Chappell T. G., Rothman J. E. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science. 1989 Jul 28;245(4916):385–390. doi: 10.1126/science.2756425. [DOI] [PubMed] [Google Scholar]
  10. Freiden P. J., Gaut J. R., Hendershot L. M. Interconversion of three differentially modified and assembled forms of BiP. EMBO J. 1992 Jan;11(1):63–70. doi: 10.1002/j.1460-2075.1992.tb05028.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gething M. J., McCammon K., Sambrook J. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell. 1986 Sep 12;46(6):939–950. doi: 10.1016/0092-8674(86)90076-0. [DOI] [PubMed] [Google Scholar]
  12. Gething M. J., Sambrook J. Protein folding in the cell. Nature. 1992 Jan 2;355(6355):33–45. doi: 10.1038/355033a0. [DOI] [PubMed] [Google Scholar]
  13. Hurtley S. M., Bole D. G., Hoover-Litty H., Helenius A., Copeland C. S. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J Cell Biol. 1989 Jun;108(6):2117–2126. doi: 10.1083/jcb.108.6.2117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kassenbrock C. K., Kelly R. B. Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides. EMBO J. 1989 May;8(5):1461–1467. doi: 10.1002/j.1460-2075.1989.tb03529.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kim P. S., Arvan P. Folding and assembly of newly synthesized thyroglobulin occurs in a pre-Golgi compartment. J Biol Chem. 1991 Jul 5;266(19):12412–12418. [PubMed] [Google Scholar]
  16. Lewis M. J., Pelham H. R. Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein. EMBO J. 1985 Dec 1;4(12):3137–3143. doi: 10.1002/j.1460-2075.1985.tb04056.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Machamer C. E., Doms R. W., Bole D. G., Helenius A., Rose J. K. Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein. J Biol Chem. 1990 Apr 25;265(12):6879–6883. [PubMed] [Google Scholar]
  18. Munro S., Pelham H. R. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell. 1986 Jul 18;46(2):291–300. doi: 10.1016/0092-8674(86)90746-4. [DOI] [PubMed] [Google Scholar]
  19. Ng D. T., Randall R. E., Lamb R. A. Intracellular maturation and transport of the SV5 type II glycoprotein hemagglutinin-neuraminidase: specific and transient association with GRP78-BiP in the endoplasmic reticulum and extensive internalization from the cell surface. J Cell Biol. 1989 Dec;109(6 Pt 2):3273–3289. doi: 10.1083/jcb.109.6.3273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Oblas B., Boyd N. D., Luber-Narod J., Reyes V. E., Leeman S. E. Isolation and identification of a polypeptide in the Hsp 70 family that binds substance P. Biochem Biophys Res Commun. 1990 Jan 30;166(2):978–983. doi: 10.1016/0006-291x(90)90907-5. [DOI] [PubMed] [Google Scholar]
  21. Palleros D. R., Reid K. L., Shi L., Welch W. J., Fink A. L. ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis. Nature. 1993 Oct 14;365(6447):664–666. doi: 10.1038/365664a0. [DOI] [PubMed] [Google Scholar]
  22. Palleros D. R., Shi L., Reid K. L., Fink A. L. hsp70-protein complexes. Complex stability and conformation of bound substrate protein. J Biol Chem. 1994 May 6;269(18):13107–13114. [PubMed] [Google Scholar]
  23. Palleros D. R., Welch W. J., Fink A. L. Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc Natl Acad Sci U S A. 1991 Jul 1;88(13):5719–5723. doi: 10.1073/pnas.88.13.5719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Pelham H. R. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell. 1986 Sep 26;46(7):959–961. doi: 10.1016/0092-8674(86)90693-8. [DOI] [PubMed] [Google Scholar]
  25. Schlossman D. M., Schmid S. L., Braell W. A., Rothman J. E. An enzyme that removes clathrin coats: purification of an uncoating ATPase. J Cell Biol. 1984 Aug;99(2):723–733. doi: 10.1083/jcb.99.2.723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Schmid D., Baici A., Gehring H., Christen P. Kinetics of molecular chaperone action. Science. 1994 Feb 18;263(5149):971–973. doi: 10.1126/science.8310296. [DOI] [PubMed] [Google Scholar]
  27. Toledo H., Carlino A., Vidal V., Redfield B., Nettleton M. Y., Kochan J. P., Brot N., Weissbach H. Dissociation of glucose-regulated protein Grp78 and Grp78-IgE Fc complexes by ATP. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2505–2508. doi: 10.1073/pnas.90.6.2505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Weissbach H., Miller D. L., Hachmann J. Studies on the role of factor Ts in polypeptide synthesis. Arch Biochem Biophys. 1970 Mar;137(1):262–269. doi: 10.1016/0003-9861(70)90433-9. [DOI] [PubMed] [Google Scholar]
  29. Welch W. J., Feramisco J. R. Rapid purification of mammalian 70,000-dalton stress proteins: affinity of the proteins for nucleotides. Mol Cell Biol. 1985 Jun;5(6):1229–1237. doi: 10.1128/mcb.5.6.1229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Zylicz M., LeBowitz J. H., McMacken R., Georgopoulos C. The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system. Proc Natl Acad Sci U S A. 1983 Nov;80(21):6431–6435. doi: 10.1073/pnas.80.21.6431. [DOI] [PMC free article] [PubMed] [Google Scholar]

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