Abstract:
:The two cardiac myosin heavy chain isoforms, alpha and beta, differ functionally, alpha Myosin exhibits higher actin-activated ATPase than does beta myosin, and hearts expressing alpha myosin exhibit increased contractility relative to hearts expressing beta myosin. To understand the molecular basis for this functional difference, we determined the complete nucleotide sequence of full-length rat alpha and beta myosin heavy chain cDNAs. This study represents the first opportunity to compare full-length fast ATPase and slow ATPase muscle myosin sequences. The alpha and beta myosin heavy chain amino acid sequences are more related to each other than to other sarcomeric myosin heavy chain sequences. Of the 1938 amino acid residues in alpha and beta myosin heavy chain, 131 are non-identical with 37 non-conservative changes. Two-thirds of these non-identical residues are clustered, and several of these clusters map to regions that have been implicated as functionally important. Some of the regions identified by the clusters of non-identical amino acid residues may affect actin binding, ATP hydrolysis and force production.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
McNally EM,Kraft R,Bravo-Zehnder M,Taylor DA,Leinwand LAdoi
10.1016/0022-2836(89)90141-1subject
Has Abstractpub_date
1989-12-05 00:00:00pages
665-71issue
3eissn
0022-2836issn
1089-8638pii
0022-2836(89)90141-1journal_volume
210pub_type
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