Analysis of the chicken fast myosin heavy chain family: Localization of isoform-specific antibody epitopes and regions of divergence

• Published in: Journal of molecular biology Vol. 225; no. 4; pp. 1143 - 1151
• Main Authors: Moore, L.A., Arrizubieta, M.J., Tidyman, W.E., Herman, L.A., Bandman, E.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 20.06.1992
• Subjects: amino acid composition; Amino Acid Sequence; Animals; Antibodies, Monoclonal; antigenic determinants; Chick Embryo; Chickens; Cloning, Molecular; divergence; DNA - genetics; DNA - isolation & purification; epitope mapping; Epitopes - analysis; Epitopes - genetics; Gene Library; Genetic Variation; heavy chains; Molecular Sequence Data; monoclonal antibody; multigene family; Muscles - physiology; myosin; myosin heavy chain; myosin isoform; Myosins - chemistry; Myosins - genetics; Myosins - immunology; Sequence Homology, Nucleic Acid; myosin heavy chain; UTR; e.l.i.s.a; MYHC; myosin isoform; monoclonal antibody; multigene family; LMM; epitope mapping; S1; bp
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/0022-2836(92)90114-Y

cDNAs encoding the rod region of four different fast myosin heavy chains (MYHCs) in the chicken were identified, using anti-MYHC monoclonal antibodies, in two expression libraries prepared from 19-day embryonic and adult chicken muscle. These clones were used to determine the amino acid sequences that encompass the epitopes of five anti-MYHC monoclonal antibodies. Additionally, the amino acid sequences were compared to each other and to a full length embryonic MYHC. Although there is extensive homology in the chicken fast myosin rods, sequences within the hinge, within the central portion of the light meromyosin fragment, and at the carboxy terminus exhibit the largest number of amino acid substitutions. We propose that divergence within these subdomains may contribute to isoform-specific properties associated with skeletal myosin rods.