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Lys‐373 of actin is involved in binding to caldesmon
Author(s) -
Kolakowski Janusz,
Makuch Robert,
Dąbrowska Renata
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80740-8
Subject(s) - caldesmon , carboxypeptidase a , carboxypeptidase , trypsin , proteolysis , amino acid residue , chemistry , biochemistry , actin , amino acid , chymotrypsin , residue (chemistry) , peptide sequence , enzyme , calmodulin , gene
Limited 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.