Complete human gene structure of obscurin: implications for isoform generation by differential splicing.

Atsushi Fukuzawa, Seraphina Idowu, Mathias Gautel

Journal: Journal of muscle research and cell motility 2007;26(6-8):427-34

PMID: 16625316

Abstract

The complete gene giant muscle protein obscurin, a modular protein composed largely of tandem Ig-domains, GDP/GTP exchange factor domains (GEF) for small G-proteins, and differentially spliced kinase domains, was analysed. The splice donor and acceptor sites of the 117 exons give important clues for potential splice pathways. The fusion of the conventional obscurin A, containing only the GEF domain, and obscurin B, fusing into the 3' kinase exons, was experimentally confirmed and analysed. The linker between the two kinases contains multiple predicted phosphorylation sites, as well as a predicted NFX zinc finger domain. Both kinases show only weak homology to either myosin light chain kinases or other giant muscle protein kinases, suggesting that they are functionally distinct.

Address: The Randall Division of Cell and Molecular Biophysics and The Cardiovascular Division, New Hunt's House, King's College London, SE1 1UL, London, United Kingdom.

DOI: 10.1007/s10974-005-9025-6

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MeSH Terms: Alternative Splicing, Amino Acid Sequence, Binding Sites, Connectin, Exons, Gene Expression Profiling, Guanine Nucleotide Exchange Factors, Humans, Molecular Sequence Data, Muscle Proteins, Myosin-Light-Chain Kinase, Phosphotransferases, Protein Isoforms, Protein Kinases, Protein Serine-Threonine Kinases, Reverse Transcriptase Polymerase Chain Reaction, Rho Guanine Nucleotide Exchange Factors, Sequence Homology, Amino Acid