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PMID: 8876186 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Interplay of structure and disorder in cochaperonin mobile loops.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 93 ·No. 21 ·1996-10-15 ·Pages 11622-7

Landry SJ, Taher A, Georgopoulos C, van der Vies SM

Abstract

Protein-protein interactions typically are characterized by highly specific interfaces that mediate binding with precisely tuned affinities. Binding of the Escherichia coli cochaperonin GroES to chaperonin GroEL is mediated, at least in part, by a mobile polypeptide loop in GroES that becomes immobilized in the GroEL/GroES/nucleotide complex. The bacteriophage T4 cochaperonin Gp31 possesses a similar highly flexible polypeptide loop in a region of the protein that shows low, but significant, amino acid similarity with GroES and other cochaperonins. When bound to GroEL, a synthetic peptide representing the mobile loop of either GroES or Gp31 adopts a characteristic bulged hairpin conformation as determined by transferred nuclear Overhauser effects in NMR spectra. Thermodynamic considerations suggest that flexible disorder in the cochaperonin mobile loops moderates their affinity for GroEL to facilitate cycles of chaperonin-mediated protein folding.

MeSH Terms
Amino Acid Sequence Binding Sites Calorimetry Chaperonin 10/chemistry,metabolism Chaperonin 60/chemistry,metabolism Entropy Escherichia coli/metabolism Hydrogen Bonding Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Peptide Fragments/chemistry,isolation & purification Peptide Mapping Protein Structure, Secondary Thermodynamics
Chemicals
Chaperonin 10 Chaperonin 60 Peptide Fragments
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Landry S J
Department of Biochemistry, Tulane University School of Medicine, New Orleans, LA 70112-2699, USA.
Taher A
Georgopoulos C
van der Vies S M
References (39)
39 references, click to expand
  1. Protein folding in the central cavity of the GroEL-GroES chaperonin complex.
    Nature. 1996 Feb 1;379(6564):420-6 PMID: 8559246
  2. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding.
    Science. 1994 Jul 29;265(5172):659-66 PMID: 7913555
  3. The universally conserved GroE (Hsp60) chaperonins.
    Annu Rev Microbiol. 1991;45:301-25 PMID: 1683763
  4. Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae.
    Science. 1996 Jan 12;271(5246):203-7 PMID: 8539620
  5. Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.
    Nature. 1994 Apr 14;368(6472):654-6 PMID: 7908418
  6. Residues in chaperonin GroEL required for polypeptide binding and release.
    Nature. 1994 Oct 13;371(6498):614-9 PMID: 7935796
  7. Conformation of beta hairpins in protein structures: classification and diversity in homologous structures.
    Methods Enzymol. 1991;202:59-82 PMID: 1784189
  8. How chaperones tell wrong from right.
    Nat Struct Biol. 1994 Dec;1(12):838-42 PMID: 7773768
  9. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.
    Anal Biochem. 1987 Nov 1;166(2):368-79 PMID: 2449095
  10. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.
    EMBO J. 1992 Dec;11(13):4757-65 PMID: 1361169
  11. Molecular chaperone functions of heat-shock proteins.
    Annu Rev Biochem. 1993;62:349-84 PMID: 8102520
  12. The crystal structure of the GroES co-chaperonin at 2.8 A resolution.
    Nature. 1996 Jan 4;379(6560):37-45 PMID: 8538739
  13. Conserved sequence motifs in bacterial and bacteriophage chaperonins.
    Trends Biochem Sci. 1995 Jan;20(1):14-5 PMID: 7878732
  14. The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S.
    Nat Struct Biol. 1996 Feb;3(2):170-7 PMID: 8564544
  15. Mutational analysis of the phage T4 morphogenetic 31 gene, whose product interacts with the Escherichia coli GroEL protein.
    Gene. 1990 Jan 31;86(1):19-25 PMID: 2311934
  16. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations.
    FEBS Lett. 1988 Mar 14;229(2):317-24 PMID: 3345845
  17. Protein-DNA interactions: how GCN4 binds DNA.
    Curr Biol. 1993 Mar;3(3):182-4 PMID: 15335794
  18. Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli.
    J Bacteriol. 1994 Nov;176(21):6558-65 PMID: 7961406
  19. Identification of 1H resonances from the bait region of human alpha 2-macroglobulin and effects of proteases and methylamine.
    Biochemistry. 1986 Sep 9;25(18):5011-7 PMID: 2429692
  20. Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association.
    Trends Biochem Sci. 1993 May;18(5):181-6 PMID: 8328018
  21. Characterization of a functionally important mobile domain of GroES.
    Nature. 1993 Jul 15;364(6434):255-8 PMID: 8100614
  22. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms.
    Cell. 1994 Aug 26;78(4):693-702 PMID: 7915201
  23. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.
    Nature. 1994 Sep 15;371(6494):261-4 PMID: 7915827
  24. 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
    Biochemistry. 1994 Mar 15;33(10):2838-42 PMID: 8130196
  25. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.
    Cell. 1996 Feb 9;84(3):481-90 PMID: 8608602
  26. Four-helix bundle growth factors and their receptors: protein-protein interactions.
    Curr Opin Struct Biol. 1995 Feb;5(1):114-21 PMID: 7773741
  27. A hot spot of binding energy in a hormone-receptor interface.
    Science. 1995 Jan 20;267(5196):383-6 PMID: 7529940
  28. Involvement of a bacterial factor in morphogenesis of bacteriophage capsid.
    Nat New Biol. 1972 Sep 13;239(89):34-7 PMID: 4561970
  29. Role of the host cell in bacteriophage morphogenesis: effects of a bacterial mutation on T4 head assembly.
    Nat New Biol. 1972 Sep 13;239(89):38-41 PMID: 4561971
  30. The structure of protein-protein recognition sites.
    J Biol Chem. 1990 Sep 25;265(27):16027-30 PMID: 2204619
  31. Modular structure of transcription factors: implications for gene regulation.
    Cell. 1991 May 31;65(5):717-9 PMID: 2040012
  32. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
    Nature. 1993 Nov 18;366(6452):228-33 PMID: 7901770
  33. Temperature dependence of the hydrophobic interaction in protein folding.
    Proc Natl Acad Sci U S A. 1986 Nov;83(21):8069-72 PMID: 3464944
  34. Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.
    Science. 1995 Aug 11;269(5225):836-41 PMID: 7638601
  35. The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
    Nature. 1994 Oct 13;371(6498):578-86 PMID: 7935790
  36. Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.
    Science. 1995 Aug 11;269(5225):832-6 PMID: 7638600
  37. Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding.
    Annu Rev Biophys Biomol Struct. 1994;23:645-69 PMID: 7919795
  38. Binding of chaperonins.
    Nature. 1991 Sep 5;353(6339):25-6 PMID: 1679197
  39. A factor preventing the major head protein of bacteriophage T4 from random aggregation.
    J Mol Biol. 1970 Jan 14;47(1):69-85 PMID: 5413343
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.93.21.11622
Published
1996-10-15
Pages
11622-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC38108
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.93.21.11622 PMC Full Text View journal details
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