Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins - PubMed (original) (raw)

Review

Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins

H Saibil. Curr Opin Struct Biol. 2000 Apr.

Abstract

Newly solved chaperone structures include the thermosome, a group II chaperonin, and a small heat-shock protein. Novel ideas on chaperone mechanism are presented in the forced unfolding hypothesis of GroEL action. Structures of chaperone-pilin complexes reveal the mechanism of chaperone interaction in bacterial pilus assembly and there have been major advances in understanding the structure and function of Hsp100 unfoldases.

PubMed Disclaimer

Similar articles

• Molecular chaperones: clamps for the Clps?
  Feng HP, Gierasch LM. Feng HP, et al. Curr Biol. 1998 Jun 18;8(13):R464-7. doi: 10.1016/s0960-9822(98)70294-5. Curr Biol. 1998. PMID: 9651675 Review.
• Here's the hook: similar substrate binding sites in the chaperone domains of Clp and Lon.
  Wickner S, Maurizi MR. Wickner S, et al. Proc Natl Acad Sci U S A. 1999 Jul 20;96(15):8318-20. doi: 10.1073/pnas.96.15.8318. Proc Natl Acad Sci U S A. 1999. PMID: 10411867 Free PMC article. No abstract available.
• A single ring is sufficient for productive chaperonin-mediated folding in vivo.
  Nielsen KL, Cowan NJ. Nielsen KL, et al. Mol Cell. 1998 Jul;2(1):93-9. doi: 10.1016/s1097-2765(00)80117-3. Mol Cell. 1998. PMID: 9702195
• Crowbars and ratchets: hsp100 chaperones as tools in reversing protein aggregation.
  Glover JR, Tkach JM. Glover JR, et al. Biochem Cell Biol. 2001;79(5):557-68. Biochem Cell Biol. 2001. PMID: 11716297 Review.
• Substrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL.
  Bhandari V, Houry WA. Bhandari V, et al. Adv Exp Med Biol. 2015;883:271-94. doi: 10.1007/978-3-319-23603-2_15. Adv Exp Med Biol. 2015. PMID: 26621473 Review.

Cited by

• Topologies of a substrate protein bound to the chaperonin GroEL.
  Elad N, Farr GW, Clare DK, Orlova EV, Horwich AL, Saibil HR. Elad N, et al. Mol Cell. 2007 May 11;26(3):415-26. doi: 10.1016/j.molcel.2007.04.004. Mol Cell. 2007. PMID: 17499047 Free PMC article.
• Proinflammatory effect in whole blood by free soluble bacterial components released from planktonic and biofilm cells.
  Oscarsson J, Karched M, Thay B, Chen C, Asikainen S. Oscarsson J, et al. BMC Microbiol. 2008 Nov 27;8:206. doi: 10.1186/1471-2180-8-206. BMC Microbiol. 2008. PMID: 19038023 Free PMC article.
• Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT.
  Booth CR, Meyer AS, Cong Y, Topf M, Sali A, Ludtke SJ, Chiu W, Frydman J. Booth CR, et al. Nat Struct Mol Biol. 2008 Jul;15(7):746-53. doi: 10.1038/nsmb.1436. Epub 2008 Jun 8. Nat Struct Mol Biol. 2008. PMID: 18536725 Free PMC article.
• AAV-mediated and pharmacological induction of Hsp70 expression stimulates survival of retinal ganglion cells following axonal injury.
  Kwong JM, Gu L, Nassiri N, Bekerman V, Kumar-Singh R, Rhee KD, Yang XJ, Hauswirth WW, Caprioli J, Piri N. Kwong JM, et al. Gene Ther. 2015 Feb;22(2):138-45. doi: 10.1038/gt.2014.105. Epub 2014 Nov 27. Gene Ther. 2015. PMID: 25427613 Free PMC article.
• The unfolding action of GroEL on a protein substrate.
  van der Vaart A, Ma J, Karplus M. van der Vaart A, et al. Biophys J. 2004 Jul;87(1):562-73. doi: 10.1529/biophysj.103.037333. Biophys J. 2004. PMID: 15240489 Free PMC article.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Elsevier Science

• Research Materials

  • NCI CPTC Antibody Characterization Program