Two distinct nonmuscle myosin‐heavy‐chain mRNAs are differentially expressed in various chicken tissues
- 1 October 1989
- journal article
- Published by Wiley in JBIC Journal of Biological Inorganic Chemistry
- Vol. 184 (3), 611-616
- https://doi.org/10.1111/j.1432-1033.1989.tb15057.x
Abstract
Two distinct cDNA clones for nonmuscle myosin heavy chain (MHC) were isolated from a chicken fibroblast cDNA library by cross-hydridization under a moderate stringency with chicken gizzard smooth muscle MHC cDNA. These two fibroblast MHC and the gizzard MHC are each encoded in different genes in the chicken genome. Northern blot analysis showed that both of the nonmuscle MHC mRNAs were expressed not only in fibroblasts but also in a variety of tissues including brain, lung, kidney, spleen, and skeletal, cardiac and smooth muscles. However, the relative contents of the two nonmuscle MHC mRNAs varied greatly among tissues. The encoded amino acid sequences of the nonmuscle MHCs were highly similar to each other (81% identity) and to the smooth muscle MHC (81-84%), but much less similar to vertebrate skeletal muscle MHCs (38-41%) or to protista nonmuscle MHCs (35-36%). A phylogenic tree of MHC isoforms was constructed by calculating the similarity scores between these MHC sequences. An examination of the tree showed that the vertebrate sarcomeric (skeletal and cardiac) MHC isoforms are encoded in a very closely related multigene family, and that the vertebrate non-sarcomeric (smooth muscle and nonmuscle) MHC isoforms define a distinct, less conserved MHC gene family.Keywords
This publication has 34 references indexed in Scilit:
- The cellular basis of myosin heavy chain isoform expression during development of avian skeletal musclesDevelopmental Biology, 1987
- Phosphorylation of myosin in non‐muscle and smooth muscle cellsFEBS Letters, 1986
- Complete nucleotide and encoded amino acid sequence of a mammalian myosin heavy chain gene: Evidence against intron-dependent evolution of the rodJournal of Molecular Biology, 1986
- Aligning amino acid sequences: Comparison of commonly used methodsJournal of Molecular Evolution, 1985
- Alkaline transfer of DNA to plastic membraneBiochemical and Biophysical Research Communications, 1984
- Structural Implications of the Myosin Amino Acid SequenceAnnual Review of Biophysics and Bioengineering, 1984
- Periodic features in the amino acid sequence of nematode myosin rodJournal of Molecular Biology, 1983
- Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin moleculesNature, 1983
- Purification and structural analysis of myosins from brain and other non-muscle tissuesJournal of Molecular Biology, 1975
- A comparison of fibroblast and smooth muscle myosinsFEBS Letters, 1974