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J. Biol. Chem., Vol. 262, Issue 30, 14625-14632, 10, 1987
M Hoshimaru and S Nakanishi
In this paper, we report the polypeptide sequence, the mRNA sequence, and
gene organization of a new category of mammalian myosin heavy chain, termed
myosin I heavy chain-like protein (MIHC), on the basis of sequence analyses
of cDNA clones isolated from a bovine intestinal cDNA library and a genomic
DNA clone containing the MIHC gene. The MIHC mRNA shares its 3' sequence
with the 5' sequence of the preprotachykinin B mRNA encoding the precursor
for the neuromedin K neuropeptide. An overlap of these functionally
unrelated mRNAs results from overlapping transcription of the same strand
of the genomic DNA sequence. The deduced amino acid sequence comprising the
amino-terminal two-thirds of the 119-kDa MIHC polypeptide is highly
homologous to that portion of conventional myosin heavy chains which forms
the globular head domain. The homology is particularly strong in the
regions of sequence thought to be involved in forming the nucleotide- and
actin-binding sites. By contrast, the deduced sequence comprising the
carboxyl-terminal one- third of MIHC shows no significant homology to that
portion of conventional myosin heavy chains which forms the alpha-helical
coiled- coil rod-like tail. In this regard, MIHC more closely resembles the
monomolecular, non-filamentous, low molecular weight myosin I heavy chain
from Acanthamoeba castellanii. Furthermore, the size of the MIHC
polypeptide, together with its preferential expression in intestinal
tissue, leads us to speculate that MIHC and the 110-kDa intestinal
brush-border protein (Collins, J. H., and Borysenko, C. W. (1984) J. Biol.
Chem. 259, 14128-14135), which binds actin and has myosin-like ATPase
activity, are the same or closely related proteins.
Identification of a new type of mammalian myosin heavy chain by molecular cloning. Overlap of its mRNA with preprotachykinin B mRNA
Institute for Immunology, Kyoto University Faculty of Medicine, Japan.
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