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Biochemistry. 1992 Dec 8;31(48):12272-6.

Trimerization of the heat shock transcription factor by a triple-stranded alpha-helical coiled-coil.

Author information

1
Department of Molecular and Cell Biology, University of California, Berkeley 94720.

Abstract

We have isolated and characterized a 91 amino acid fragment of the heat shock transcription factor from both Saccharomyces cerevisiae and Kluyveromyces lactis. The two protein fragments behave similarly: they form homotrimers, as indicated by sedimentation equilibrium and cross-linking, and contain approximately 80% alpha-helix, as indicated by circular dichroism. Sedimentation velocity and diffusion coefficients indicate that they have an elongated, nonspherical shape. We conclude the following: these fragments contain a domain which forms a trimer via a triple-stranded alpha-helical coiled-coil, similar to that found in influenza hemagglutinin.

PMID:
1457424
DOI:
10.1021/bi00163a042
[Indexed for MEDLINE]

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