Trimerization of the heat shock transcription factor by a triple-stranded alpha-helical coiled-coil.
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.
Peteranderl
R
R
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Nelson
H C
HC
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D000076249:Heat Shock Transcription Factors; D007716:Kluyveromyces / Q000737:chemistry; D008027:Light; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000737:chemistry; D012542:Scattering, Radiation; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics
D004268:DNA-Binding Proteins; D000076249:Heat Shock Transcription Factors; D010446:Peptide Fragments; D014157:Transcription Factors