J. Anim Sci.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J. Anim Sci. 1986. 63:259-268.
© 1986 American Society of Animal Science

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Young, R. B.
Right arrow Articles by McGee, C. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Young, R. B.
Right arrow Articles by McGee, C. E.

Structural Analysis of Myosin Genes Using Recombinant DNA Techniques1,2,

Ronald B. Young, Debra M. Moriarity and Christopher E. McGee

University of Alabama3, Huntsville 35899

Abstract

Myosin, the major protein of the myofibril, consists of two heavy chains with a molecular weight (MW) of 200,000, complexed with four light chains of MW 17,000 to 21,000. Both the heavy and light chains exhibit polymorphisms that are tissue-specific and developmental stage-specific. Myosin heavy chains and light chains appear to be represented in the genome as multigene families in various species, including chickens, cattle, humans, rats, rabbits and nematodes. Myosin heavy-chain proteins have a high amino acid sequence homology among isoforms, and the genes for each isoform likewise exhibit a high degree of nucleotide sequence conservation. The myosin heavy-chain genes have a complex structure and contain up to 65% intervening sequence composed of up to 20 or more individual introns. Partial sequence data, transcriptional orientation and tissue of expression have been determined for several myosin heavy-chain genes. The use of recombinant DNA and associated techniques will eventually yield definitive information on the control of expression of each individual gene, as well as factors that regulate expression of closely related isoforms.


Footnotes

1 This effort was supported in part by a research grant from NIH (AM01095).

2 Presented by the senior author at a symposium on "Future Impact of Biotechnology in Animal Science," held August 14, 1985 at the 77th Annu. Meet. of the Amer. Soc. of Anim. Sci., Univ. of Georgia, Athens.

3 Dept. of Biol. Sci.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1986 by the American Society of Animal Science.