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

作者：Ralph Peteranderl, Hillary C.M. Nelson · 发表于：Biochemistry · 年份：1992 · DOI：10.1021/bi00163a042 · 被引用次数：145 · 研究领域：Heat shock proteins research、RNA Research and Splicing、RNA and protein synthesis mechanisms

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.