Rb. Young et al., EXPRESSION PATTERN AND PARTIAL SEQUENCE-ANALYSIS OF A FETAL BOVINE MYOSIN HEAVY-CHAIN GENE, Journal of animal science, 72(4), 1994, pp. 903-910
A fragment of a bovine myosin heavy-chain (MHC) gene approximately 15
kbp in size (designated MHC 67) was isolated from a bovine genomic DNA
library. The direction of transcription was determined, and prelimina
ry experiments indicated that the gene was expressed in fetal skeletal
muscle. The expression pattern of this gene was, therefore, evaluated
in detail using northern blots containing RNA from eleven different b
ovine muscle and nonmuscle tissues at three developmental ages. A rest
riction fragment of clone MHC 67 containing the 3' untranslated sequen
ce (which is specific for each MHC gene) was used as a probe. This gen
e fragment hybridized predominantly to RNA from fetal skeletal muscles
and did not hybridize to RNA from either neonatal or adult skeletal m
uscles (red or white), smooth muscle tissue, or nonmuscle tissue. A 7-
kb EcoRI fragment containing both translated and untranslated regions
surrounding the 3' end of the gene was subcloned into pBluescript II K
S+ and partially sequenced. When these bovine sequences were aligned t
o that of the human and rat skeletal and cardiac MHC genes, we found t
hat these sequences corresponded to exons 31, 32, and 33, and that the
y had homology with human perinatal and fetal MHC as high as 90% at th
e nucleotide level and 97% at the amino acid level. Comparison of the
nucleotide sequences of isoform-specific 3' nontranslated regions from
bovine, human, and rat genes further verify that the MHC 67 clone enc
odes the bovine fetal or perinatal MHC isoform.