The Primary Structure of Skeletal Muscle Myosin Heavy Chain: IV. Sequence of the Rod, and the Complete 1,938-Residue Sequence of the Heavy Chain

Abstract

In the preceding paper [Maita, T., Miyanishi, T., Matsuzono, K., Tanioka, Y., & Matsuda, G. (1991) J. Biochem. 110, 68-74], we reported the amino-terminal 837-residue sequence of the heavy chain of adult chicken pectoralis muscle myosin. This paper describes the carboxyl terminal 1,097-residue sequence and the linkage of the two sequences. Rod obtained by digesting myosin filaments with alpha-chymotrypsin was redigested with the protease at high KCl concentration, and two fragments, subfragment-2 and light meromyosin, were isolated and sequenced by conventional methods. The linkage of the two fragments was deduced from the sequence of an overlapping peptide obtained by cleaving the rod with cyanogen bromide. The rod contained 1,039 amino acid residues, but lacked the carboxyl-terminal 58 residues of the heavy chain. A carboxyl-terminal 63-residue peptide obtained by cleaving the whole heavy chain with cyanogen bromide was sequenced. Thus, the carboxyl terminal 1,097-residue sequence of the heavy chain was completed. The linkage of subfragment-1 and the rod was deduced from the sequence of an overlapping peptide between the two which was obtained by cleaving heavy meromyosin with cyanogen bromide. Comparing the sequence of the adult myosin thus determined with that of chicken embryonic myosin reported by Molina et al. [Molina, M.I., Kropp, K.E., Gulick, J., & Robbins, J. (1987) J. Biol. Chem. 262, 6478-6488], we found that the sequence homology is 94%.

Myo3A, One of Two Class III Myosin Genes Expressed in Vertebrate Retina, Is Localized to the Calycal Processes of Rod and Cone Photoreceptors and Is Expressed in the Sacculus

“…All six members of the class III myosins, bass Myo3A and Myo3B, human MYO3A (Dosé and Burnside, 2000) and MYO3B (Dosé and Burnside, 2002), Drosophila NINAC (Montell and Rubin, 1988), and Limulus MyoIII LIM (Battelle et al, 1998) are compared with one to three representative members of all other myosin classes. The comparison spans the motor domain region corresponding to amino acids 88 -780 of chicken muscle myosin (Gg II) (Maita et al, 1991), similar to previously published myosin trees (Cope et al, 1996;Hodge and Cope, 2000).…”

Effect of ultrasonication on secondary structure and heat induced gelation of chicken myofibrils

“…4 The change of surface hydrophobicity of myofibrils treated with low frequency ultrasonication sulphonic acid (ANS) has been found to bind hydrophobic amino acids on unfolded myosin molecule (Benjakul et al 1997), surface hydrophobicity can be used as an indicator of conformational changes occurring in myofibril proteins, specifically in myosin. Moreover, it is reported that myosin head is richer in hydrophobic residues (Maita et al 1991), therefore marked increase in hydrophobicity observed at 20 min and 30 min indicated significant exposure of hydrophobic residues in head region of myosin. A significant decrease in Ca 2?…”

Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy.

“…The locations of the amino acid mutations were mapped onto the chicken structure by aligning the sequences of the human cardiac and chicken skeletal muscle myosins with the GCG program package (25). There was 79% sequence identity between the two proteins in their respective myosin heads (26,27).…”