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Nucleic Acids Research, 1990, Vol. 18, No. 11 3147-3153
© 1990

MOLECULAR BIOLOGY

A bovine homolog to the human myogenic determination factor myf-5: sequence conservation and 3' processing of transcripts

Theodore G. Clark, Julie Morris, Maho Akamatsu1, Royal A. McGraw1 and Robert Ivarie*

Department of Genetics , University of Georgia Athens, GA 30602, USA 1Department of Physiology and Pharmacology, University of Georgia ,Athens, GA 30602, USA

*To whom correspondence should be addressed

Accepted April 26, 1990.

A bovine cDNA library from fetal skeletal muscle myoblasts.was screened with a 274 bp probe to a conserved region of the mouse MyoD1 cDNA. One positive recombinant, designated bmyf, was found to contain a 1931 bp Insert with an open reading frame encoding a predicted protein highly related to the human myogenic factor myf–5 Human and bovine factors are 96% homologous in their predicted amlno acid sequences. At the nucleotlde level, bmyf and myf–5 are 92% identical in the coding region and 74 and 80% homologous in their 5'- and 3'-untranslated regions, respectively. The bmyf cDNA, nevertheless, extends 475 nucleotides beyond a polyadenylation signal common to both cDNAs. Bmyf transcripts are expressed exclusively in skeletal muscle where three transcripts of 1.5, 2 and 3 kb were detected. While the 1.5 kb transcript lacks sequences 3' to the polyadenylation signal at nt 1415 In the bmyf cONA, both the 2 and 3 kb RNAs contain these sequences suggesting that bmyf transcripts are alternatively polyadenylated. Bmyf cDNA can activate the expression of the myogenic program in C3H10T1/2 fibroblasts as assayed by stable and transient transfection experiments.


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