Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84) - PubMed (original) (raw)

Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)

R Shaknovich et al. Mol Cell Biol. 1992 Nov.

Abstract

A murine cardiac lambda gt11 expression library was screened with an amphipathic helix antibody, and a recombinant representing the C-terminal 194 residues of murine HSP90 (HSP84) was cloned. Both recombinant and native HSP90s were then found to rapidly convert a basic helix-loop-helix protein (MyoD1) from an inactive to an active conformation, as assayed by sequence-specific DNA binding. The conversion process involves a transient interaction between HSP90 and MyoD1 and does not result in the formation of a stable tertiary complex. Conversion does not require ATP and occurs stoichiometrically in a dose-dependent fashion. HSP90 is an abundant, ubiquitous, and highly conserved protein present in most eukaryotic cells. These results provide direct evidence that HSP90 can affect the conformational structure of a DNA-binding protein.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Annu Rev Biochem. 1978;47:251-76 - PubMed
    1. Nature. 1992 Jan 2;355(6355):33-45 - PubMed
    1. Cell. 1991 Jul 26;66(2):191-7 - PubMed
    1. J Biol Chem. 1990 Aug 5;265(22):12778-81 - PubMed
    1. Gene. 1987;56(1):29-40 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources