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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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| Published in: | The Journal of biological chemistry 1996-08, Vol.271 (32), p.19042-19052 |
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| Main Authors: | , , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c415t-4264b55a5859e3facada3bf054ee359a7c9f77822cfd5ca50c15cb4855a2bce43 |
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| cites | cdi_FETCH-LOGICAL-c415t-4264b55a5859e3facada3bf054ee359a7c9f77822cfd5ca50c15cb4855a2bce43 |
| container_end_page | 19052 |
| container_issue | 32 |
| container_start_page | 19042 |
| container_title | The Journal of biological chemistry |
| container_volume | 271 |
| creator | Bantle, S. (Swiss Federal Institute of Technology, Zurich, Switzerland.) Keller, S Haussmann, I Auerbach, D Perriard, E Muhlebach, S Perriard, J.C |
| description | 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 |
| doi_str_mv | 10.1074/jbc.271.32.19042 |
| format | article |
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(Swiss Federal Institute of Technology, Zurich, Switzerland.) ; Keller, S ; Haussmann, I ; Auerbach, D ; Perriard, E ; Muhlebach, S ; Perriard, J.C</creator><creatorcontrib>Bantle, S. (Swiss Federal Institute of Technology, Zurich, Switzerland.) ; Keller, S ; Haussmann, I ; Auerbach, D ; Perriard, E ; Muhlebach, S ; Perriard, J.C</creatorcontrib><description>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. 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(Swiss Federal Institute of Technology, Zurich, Switzerland.)</creatorcontrib><creatorcontrib>Keller, S</creatorcontrib><creatorcontrib>Haussmann, I</creatorcontrib><creatorcontrib>Auerbach, D</creatorcontrib><creatorcontrib>Perriard, E</creatorcontrib><creatorcontrib>Muhlebach, S</creatorcontrib><creatorcontrib>Perriard, J.C</creatorcontrib><title>Tissue-specific isoforms of chicken myomesin are generated by alternative splicing</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>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. 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(Swiss Federal Institute of Technology, Zurich, Switzerland.)</au><au>Keller, S</au><au>Haussmann, I</au><au>Auerbach, D</au><au>Perriard, E</au><au>Muhlebach, S</au><au>Perriard, J.C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tissue-specific isoforms of chicken myomesin are generated by alternative splicing</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1996-08-09</date><risdate>1996</risdate><volume>271</volume><issue>32</issue><spage>19042</spage><epage>19052</epage><pages>19042-19052</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>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. 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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1996-08, Vol.271 (32), p.19042-19052 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | ScienceDirect - Connect here FIRST to enable access |
| 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 |
| title | Tissue-specific isoforms of chicken myomesin are generated by alternative splicing |
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