Ligands regulate GroEL thermostability.

Abstract:

:Escherichia coli heat-shock proteins GroEL and GroES stimulate (in an ATP-dependent manner) the folding of various proteins. In this study scanning microcalorimetry was applied to investigate GroEL thermostability in the presence of its ligands. Mg2+ and K+ ions stabilize while ADP destabilizes the GroEL molecule against the action of temperature. Furthermore, ADP essentially increases the number of binding sites for the hydrophobic probe (ANS) and the number of GroEL SH-groups accessible to Ellman's reagent as well as the accessibility of the protein to the action of trypsin. The interaction of GroEL with GroES in the presence of Mg2+-ADP eliminates the destabilizing effect of ADP on the GroEL molecule against the action of temperature and Ellman's reagent but does not change its hydrophobicity and accessibility to trypsin.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Surin AK,Kotova NV,Kashparov IA,Marchenkov VV,Marchenkova SYu,Semisotnov GV

doi

10.1016/s0014-5793(97)00199-3

subject

Has Abstract

pub_date

1997-04-01 00:00:00

pages

260-2

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014579397001993

journal_volume

405

pub_type

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