Primary structure and functional expression of h-caldesmon complementary DNA

Biochem Biophys Res Commun. 1989 Oct 16;164(1):503-11. doi: 10.1016/0006-291x(89)91748-8.

Abstract

Recently, the two Mr forms of caldesmon (Mr's in the range of 120-150kDa and 70-80kDa as judged by SDS-PAGE) have been identified. h-Caldesman (high Mr 120-150kDa caldesmon) is predominantly expressed in smooth muscles, and l-caldesmon (low Mr 70-80kDa caldesmon) in non-muscle cells. In this paper, we report the nucleotide sequence of chick embryo gizzard h-caldesmon cDNA and its translation into amino acid sequence. This sequence predicts a protein of 771 amino acids with a Mr of 88,743. The central portion of this sequence is composed of a 10-fold repeat of conserved amino acid sequence containing 13-15 amino acids. Further, a recombinant protein produced in Escherichia coli containing the full-length h-caldesmon cDNA has been characterized. Although the Mr of h-caldesmon predicted from amino acid sequence is 88,743, native and recombinant proteins show the same mol. wt. with 150kDa as measured by SDS-PAGE. This discrepancy may be due to the acidic amino acid-rich sequences at the N-terminal and central portions. A recombinant protein produced in E. coli possesses calmodulin-, F-actin- and tropomyosin-binding abilities in common with the native h-caldesmon.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Calmodulin-Binding Proteins / genetics*
  • Chickens
  • Cloning, Molecular
  • DNA / genetics*
  • Electrophoresis, Polyacrylamide Gel
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Plasmids
  • Recombinant Proteins / analysis
  • Repetitive Sequences, Nucleic Acid

Substances

  • Calmodulin-Binding Proteins
  • Recombinant Proteins
  • DNA