Abstract
Binding of heat-shock protein (hsp70) to polymerized tubulin has been investigated by in vitro experiments. The tubulin region involved in binding to hsp70 corresponds to the carboxy-terminal residues 431-444, also involved in the association with other microtubule-associated proteins (MAPs). Additionally, the putative tubulin binding motif in the hsp70 protein contains a sequence related to the motif described for MAP1B protein.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding, Competitive
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Brain / metabolism
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Cattle
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Cloning, Molecular
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Electrophoresis, Polyacrylamide Gel
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Heat-Shock Proteins / chemistry
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Heat-Shock Proteins / isolation & purification
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Heat-Shock Proteins / metabolism*
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Humans
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Kinetics
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Microtubule Proteins / chemistry
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Microtubule Proteins / metabolism
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Molecular Sequence Data
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Molecular Weight
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Peptide Fragments / chemical synthesis
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Protein Biosynthesis
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Rabbits
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Reticulocytes / metabolism
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Transcription, Genetic
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Tubulin / chemistry
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Tubulin / isolation & purification
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Tubulin / metabolism*
Substances
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Heat-Shock Proteins
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Microtubule Proteins
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Peptide Fragments
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Recombinant Proteins
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Tubulin