Binding of heat-shock protein 70 (hsp70) to tubulin

Arch Biochem Biophys. 1994 May 1;310(2):428-32. doi: 10.1006/abbi.1994.1188.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding, Competitive
  • Brain / metabolism
  • Cattle
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / isolation & purification
  • Heat-Shock Proteins / metabolism*
  • Humans
  • Kinetics
  • Microtubule Proteins / chemistry
  • Microtubule Proteins / metabolism
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Biosynthesis
  • Rabbits
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Reticulocytes / metabolism
  • Transcription, Genetic
  • Tubulin / chemistry
  • Tubulin / isolation & purification
  • Tubulin / metabolism*

Substances

  • Heat-Shock Proteins
  • Microtubule Proteins
  • Peptide Fragments
  • Recombinant Proteins
  • Tubulin