Isoform-specific interaction of the myosin-binding proteins (MyBPs) with skeletal and cardiac myosin is a property of the C-terminal immunoglobulin domain

被引:52
作者
Alyonycheva, TN
Mikawa, T
Reinach, FC
Fischman, DA
机构
[1] CORNELL UNIV,COLL MED,DEPT CELL BIOL & ANAT,NEW YORK,NY 10021
[2] UNIV SAO PAULO,INST QUIM,DEPT BIOQUIM,BR-01498 SAO PAULO,BRAZIL
关键词
D O I
10.1074/jbc.272.33.20866
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Full-length cDNAs encoding chicken and human skeletal MyBP-H and MyBP-C have been isolated and sequenced (1-5). All are members of a protein family with repetitive immunoglobulin C2 and fibronectin type III motifs. The myosin binding domain was mapped to a single immunoglobulin motif in cardiac MyBP-C and skeletal MyBP-H. Limited alpha-chymotryptic digestion of cardiac MyBP-C generated three peptides, similar in relative mobility to those of skeletal MyBP-C: similar to 100, 40, and 15 kDa. Tryptic digestion of MyBP-H yielded two peptides: similar to 50 and 14 kDa. Partial amino acid sequences proved that the 15 and 14-kDa fragments are located at the C termini of cardiac MyBP-C and skeletal My PP-H, respectively. Only the 14- and 15-kDa peptides bound to myosin. Thus, the myosin binding site in all three proteins resides within an homologous, C-terminal immunoglobulin domain. Binding reactions (2) between the skeletal and cardiac MyBPs and corresponding myosin isoforms demonstrated saturable binding of the MyBP proteins and their C-terminal peptides to myosin, but there are higher limiting stoichiometries with the homologous isoform partners. Evidence is presented indicating that MS BP-H and -C compete for binding to a discrete number of sites in myosin filaments.
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页码:20866 / 20872
页数:7
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