The importance of C-terminal amino acid residues of actin to the inhibition of actomyosin ATPase activity by caldesmon and troponin I

FEBS Lett. 1992 Feb 10;297(3):237-40. doi: 10.1016/0014-5793(92)80546-s.

Abstract

Proteolytic elimination of three C-terminal amino acid residues from actin weakens its interaction with caldesmon and troponin I and, in consequence, lowers the inhibitory effects of both proteins on actomyosin ATPase activity. These results prove the importance of C-terminal extremity of actin to the overall interaction of this protein with caldesmon and troponin I.

MeSH terms

  • Actins / chemistry*
  • Actins / physiology
  • Animals
  • Ca(2+) Mg(2+)-ATPase / metabolism
  • Calmodulin-Binding Proteins / physiology*
  • Chickens
  • Enzyme Activation
  • Myosins / antagonists & inhibitors*
  • Troponin / physiology*
  • Troponin I

Substances

  • Actins
  • Calmodulin-Binding Proteins
  • Troponin
  • Troponin I
  • Ca(2+) Mg(2+)-ATPase
  • Myosins