Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84).
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.
Mesh Terms:
Allosteric Regulation, Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Escherichia coli, Heat-Shock Proteins, Mice, Molecular Sequence Data, MyoD Protein, Nuclear Proteins, Phosphoproteins, Protein Binding, Protein Conformation, Protein Denaturation, Sequence Homology, Amino Acid
Allosteric Regulation, Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Escherichia coli, Heat-Shock Proteins, Mice, Molecular Sequence Data, MyoD Protein, Nuclear Proteins, Phosphoproteins, Protein Binding, Protein Conformation, Protein Denaturation, Sequence Homology, Amino Acid
Mol. Cell. Biol.
Date: Nov. 01, 1992
PubMed ID: 1406681
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