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Binding of heptapeptides or unfolded proteins to the chimeric C-terminal domains of 70-kDa heat shock cognate protein.

Abstract
Seventy-kDa heat shock cognate protein (hsc70) and its homologs in bacteria, yeast and vertebrates are known to form complexes with S-carboxymethyl-alpha-lactalbumin (CMLA), an unfolded protein; and, this activity has been attributed to its C-terminal 30-kDa domain. Herein, we show that hsc70s isolated from the seeds of mung bean and peas, however, are not effective in complexing with CMLA, and that the 30-kDa domain of Arabidopsis hsc70 (At30) cannot form stable complexes with CMLA either. Moreover, chimeric 30-kDa domains, either composed of rat 18-kDa and Arabidopsis 10-kDa subdomains (R18At10) or with Arabidopsis 18-kDa and rat 10-kDa subdomains (At18R10), were prepared and tested for their ability to complex with CMLA or a heptapeptide FYQLALT. At18R10 cannot complex with both CMLA and FYQLALT. On the other hand, R18At10 is capable of forming complexes with FYQLALT at a level similar to that of the rat 30-kDa domain (R30). R18At10 also forms complexes with CMLA, but the amount of the R18At10/CMLA complexes is much less than that of R30/CMLA. The results imply that the 18-kDa subdomain dictates the binding specificity for heptapeptide, and that the C-terminal 10-kDa subdomain may also provide some selection or restriction for unfolded proteins to form complexes with hsc70.
AuthorsS J Wu, C Wang
JournalEuropean journal of biochemistry (Eur J Biochem) Vol. 259 Issue 1-2 Pg. 449-55 (Jan 1999) ISSN: 0014-2956 [Print] England
PMID9914526 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Carrier Proteins
  • HSC70 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • Hspa8 protein, rat
  • Oligopeptides
  • Peptide Fragments
  • Recombinant Fusion Proteins
  • Lactalbumin
Topics
  • Amino Acid Sequence
  • Animals
  • Arabidopsis
  • Binding Sites
  • Carrier Proteins (genetics, metabolism)
  • HSC70 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins (genetics, metabolism)
  • Lactalbumin (analogs & derivatives, metabolism)
  • Molecular Sequence Data
  • Oligopeptides (metabolism)
  • Peptide Fragments (genetics, metabolism)
  • Protein Binding
  • Protein Conformation
  • Rats
  • Recombinant Fusion Proteins (metabolism)
  • Sequence Homology, Amino Acid

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