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(Received for publication, March 12, 1997, and in revised form, May 15, 1997)
From the 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
Volume 272, Number 33,
Issue of August 15, 1997
pp. 20866-20872
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
and
Department of Cell Biology and Anatomy,
Cornell University Medical College, New York, New York 10021 and the
Department Bioquimica, Instituto de Quimica, Universidade de
São Paulo, CP 20.780, CEP 01498, São Paulo, Brazil
-chymotryptic digestion of cardiac MyBP-C generated three
peptides, similar in relative mobility to those of skeletal MyBP-C:
~100, 40, and 15 kDa. Tryptic digestion of MyBP-H yielded two
peptides: ~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 MyBP-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 MyBP-H and -C compete
for binding to a discrete number of sites in myosin filaments.
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