Lys‐373 of actin is involved in binding to caldesmon
1992; Wiley; Volume: 309; Issue: 1 Linguagem: Inglês
10.1016/0014-5793(92)80740-8
ISSN1873-3468
AutoresJanusz Kołakowski, Robert Makuch, Renata Da̧browska,
Tópico(s)Cardiomyopathy and Myosin Studies
ResumoLimited proteolysis of actin with trypsin removes its two or three C‐terminal amino acid residues [Proc. Natl. Acad. Sci. USA 81 (1984) 3680–3684]. Carboxypeptidase B‐treatment of G‐ and F‐actin previously digested with trypsin revealed that in the first case preferential release of three and in the second two C‐terminal amino acid residues takes place. Tryptic removal of three but not two C‐terminal amino acid residues of actin causes weakening of its interaction with caldesmon and lowering of the caldesmon‐induced inhibitory effect on actomyosin ATPase activity. Therefore, it is concluded that the third amino acid residue from the C terminus of actin, Lys‐373, is important for the interaction with caldesmon.
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