Document Detail


Isoform-specific interaction of the myosin-binding proteins (MyBPs) with skeletal and cardiac myosin is a property of the C-terminal immunoglobulin domain.
MedLine Citation:
PMID:  9252413     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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: approximately 100, 40, and 15 kDa. Tryptic digestion of MyBP-H yielded two peptides: approximately 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.
Authors:
T N Alyonycheva; T Mikawa; F C Reinach; D A Fischman
Related Documents :
19920153 - Troponin regulatory function and dynamics revealed by h/d exchange-mass spectrometry.
12972413 - Spatial and dynamic interactions between phospholamban and the canine cardiac ca2+ pump...
6788893 - Binding of bacillus calmette-guérin-activated macrophages to tumor targets. selective ...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  272     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1997 Aug 
Date Detail:
Created Date:  1997-09-04     Completed Date:  1997-09-04     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  20866-72     Citation Subset:  IM    
Affiliation:
Department of Cell Biology and Anatomy, Cornell University Medical College, New York, New York 10021, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Binding Sites
Binding, Competitive
Carrier Proteins / metabolism*
Chickens
Immunoglobulins / metabolism*
Molecular Sequence Data
Molecular Weight
Muscle, Skeletal / metabolism
Myocardium / metabolism
Myosins / metabolism*
Peptide Fragments / metabolism*
Grant Support
ID/Acronym/Agency:
AR32147/AR/NIAMS NIH HHS
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Immunoglobulins; 0/Peptide Fragments; EC 3.6.4.1/Myosins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Ca2+/calmodulin causes Rab3A to dissociate from synaptic membranes.
Next Document:  Role of the yeast phosphatidylinositol/phosphatidylcholine transfer protein (Sec14p) in phosphatidyl...