Tissue-specific isoforms of chicken myomesin are generated by alternative splicing

Myomesin is a high molecular weight protein that is present in the M-band of all fiber types of cross-striated skeletal muscle and heart. We have isolated two cDNAs encoding tissue-specific isoforms of chicken myomesin with calculated molecular masses of 174 kDa in skeletal muscle and 182 kDa in hea...

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Bibliographic Details
Published in:The Journal of biological chemistry 1996-08, Vol.271 (32), p.19042-19052
Main Authors: Bantle, S. (Swiss Federal Institute of Technology, Zurich, Switzerland.), Keller, S, Haussmann, I, Auerbach, D, Perriard, E, Muhlebach, S, Perriard, J.C
Format: Article
Language:English
Subjects:
ADN
Alternative Splicing
Amino Acid Sequence
Animals
Base Sequence
Chickens
Cloning, Molecular
COEUR
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
Connectin
CORAZON
DNA, Complementary
Humans
Molecular Sequence Data
MUSCLE
Muscle Proteins - genetics
Muscle, Skeletal - metabolism
MUSCULOS
Myocardium - metabolism
POLLO
POULET
Protein Conformation
PROTEINAS
PROTEINE
Rats
RNA, Messenger - genetics
SECUENCIA NUCLEOTIDICA
Sequence Homology, Amino Acid
SEQUENCE NUCLEOTIDIQUE
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Summary:Myomesin is a high molecular weight protein that is present in the M-band of all fiber types of cross-striated skeletal muscle and heart. We have isolated two cDNAs encoding tissue-specific isoforms of chicken myomesin with calculated molecular masses of 174 kDa in skeletal muscle and 182 kDa in heart. Distinct sequences are found at the 3'-end of the two cDNAs, giving rise to different C-terminal domains. Partial analysis of the gene structure has shown that in chicken, both isoforms are generated by alternative splicing of a composite exon. Amino acid sequences show that the main body of myomesin consists of five fibronectin type III (class I motifs) and seven immunoglobulin-like domains (class II motifs). An identical structure was found in M-protein and human 190K protein (the human counterpart of chicken myomesin), and a comparable domain arrangement occurs in the M-band-associated protein skelemin. We postulate that myomesin, M-protein, and skelemin belong to the same subfamily of high molecular weight M-band-associated proteins of the immunoglobulin superfamily and that they probably have the same ancestor in evolution
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.271.32.19042