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Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding.

Authors
  • Motojima, F
  • Makio, T
  • Aoki, K
  • Makino, Y
  • Kuwajima, K
  • Yoshida, M
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Jan 27, 2000
Volume
267
Issue
3
Pages
842–849
Identifiers
PMID: 10673379
Source
Medline
License
Unknown

Abstract

The GroES binding site at the apical domain of GroEL, mostly consisting of hydrophobic residues, overlaps largely with the substrate polypeptide binding site. Essential contribution of hydrophobic interaction to the binding of both GroES and polypeptide was exemplified by the mutant GroEL(L237Q) which lost the ability to bind either of them. The binding site, however, contains three hydrophilic residues, E238, T261, and N265. For GroES binding, N265 is essential since GroEL(N265A) is unable to bind GroES. E238 contributes to rapid GroES binding to GroEL because GroEL(E238A) is extremely sluggish in GroES binding. Polypeptide binding was not impaired by any mutations of E238A, T261A, and N265A. Rather, these mutants, especially GroEL(N265A), showed stronger polypeptide binding affinity than wild-type GroEL. Thus, these hydrophilic residues have a dual role; they help GroES binding on one hand but attenuate polypeptide binding on the other hand.

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