Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain

S. Yu Khaitlina, J. H. Collins, I. M. Kuznetsova, V. P. Pershina, I. G. Synakevich, K. K. Turoverov, A. M. Usmanova

Research output: Contribution to journalArticle

53 Scopus citations

Abstract

The 36 kDa fragment of actin molecule obtained with the protease from E. coli A2 strain [(1988) FEBS Lett. 228, 172] was shown to begin with Val-43 and retain the COOH-terminal amino acid residues of the parent molecule. The E. coli protease split actin preserves the NH2-terminal part of the polypeptide chain as well as the native conformation of actin molecule. However, the E. coli protease split actin failed to polymerize in 0.1 M KCl, suggesting that integrity of actin molecule between Gly-42 and Val-43 is crucial for actin polymerization.

Original languageEnglish (US)
Pages (from-to)49-51
Number of pages3
JournalFEBS Letters
Volume279
Issue number1
DOIs
StatePublished - Feb 11 1991

Keywords

  • Bacterial protease
  • Intrinsic fluoroscence
  • Split actin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Khaitlina, S. Y., Collins, J. H., Kuznetsova, I. M., Pershina, V. P., Synakevich, I. G., Turoverov, K. K., & Usmanova, A. M. (1991). Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain. FEBS Letters, 279(1), 49-51. https://doi.org/10.1016/0014-5793(91)80247-Z