title: Identification of a novel smooth muscle myosin heavy chain cDNA: isoform diversity in the S1 head region.
abstract: Smooth muscle myosin heavy chain (SMHC) isoforms, SM1 and SM2, are the products of alternative splicing from a single gene (P. Babij and M. Periasamy. J. Mol. Biol. 210: 673-679, 1989). We have previously shown that this splicing occurs at the 3'-end of the mRNA, resulting in proteins that differ at the carboxyterminal (R. Nagai, M. Kuro-o, P. Babij, and M. Periasamy. J. Biol. Chem. 264: 9734-9737, 1989). In the present study we demonstrate that additional SMHC isoform diversity occurs in the globular head region by isolating and characterizing two distinct rat SMHC cDNA (SMHC-11 = SM1B and SMHC-5 = SM1A). Sequence comparison of the two clones reveals that they are completely identical in their coding regions, except at the region encoding the 25/50 kDa junction of the myosin head, where the SM1B isoform contains an additional seven amino acids. This divergent region is located adjacent to the Mg(2+)-ATPase site, and differences in this region may be of functional importance. Ribonuclease protection analysis demonstrates that the corresponding SM1B and SM1A mRNA messages are coexpressed in all smooth muscle tissues; however, the proportion of the two mRNA present differs significantly between tissues. The SM1A-type mRNA predominates in most smooth muscle tissues, with the exception of intestine and urinary bladder, which contain greater proportions of the SM1B message. The differential distribution of these two isoforms may provide important clues toward understanding differences in smooth muscle contractile properties.
authors.affiliation: Department of Physiology and Biophysics, University of Vermont College of Medicine, Burlington 05405-0068.
authors.forename: S
authors.initials: S
authors.lastname: White
authors.forename: A F
authors.initials: AF
authors.lastname: Martin
authors.forename: M
authors.initials: M
authors.lastname: Periasamy
mesh_terms: D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017301:Ca(2+) Mg(2+)-ATPase / Q000235:genetics / Q000378:metabolism; D002645:Chickens; D004247:DNA / Q000235:genetics* / Q000302:isolation & purification; D005260:Female; D005333:Fetus; D015723:Gene Library; D014644:Genetic Variation; D007422:Intestines / Q000502:physiology; D008969:Molecular Sequence Data; D009130:Muscle, Smooth / Q000502:physiology*; D009218:Myosins / Q000235:genetics*; D009838:Oligodeoxyribonucleotides; D009928:Organ Specificity; D012313:RNA / Q000235:genetics / Q000302:isolation & purification; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D011817:Rabbits; D051381:Rats; D017386:Sequence Homology, Amino Acid; D001743:Urinary Bladder / Q000502:physiology
chemical_list: D009838:Oligodeoxyribonucleotides; D012333:RNA, Messenger; D012313:RNA; D004247:DNA; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins