Structural organization and expression of the gene for bovine myosin I heavy chain.
Brush border myosin I heavy chain (MIHC), known previously as the brush border 110-kDa protein, contains an amino-terminal sequence which is highly homologous to the globular head domain of conventional myosin II heavy chain (MIIHC). The carboxyl-terminal sequence of MIHC completely diverges from that of MIIHC and functions as calmodulin-binding and membrane-interaction sites. In this investigation, we determined the structural organization of the bovine MIHC by isolating a set of genomic segments containing the whole MIHC gene. The bovine MIHC gene is 26 kilobase pairs long and consists of 28 exons. At the homologous amino-terminal portion of MIHC, many introns are located at positions equivalent to those of the rat MIIHC gene and the amoeba MIHC gene. At the carboxyl-terminal sequence of MIHC, the putative calmodulin-binding and membrane-interacting domains are specified by discrete sets of exons. These findings support the view that the amino-terminal head portions of MIHC and MIIHC evolved from a common ancestral origin and also that the MIHC protein was generated as a result of fusion of discrete genomic segments encoding different functional and structural protein domains. Analysis of tissue expression of the MIHC mRNA was also extended in this investigation, and the results indicated that this mRNA is expressed in some tissues other than the intestines.
Kawakami
H
H
Institute for Immunology, Kyoto University Faculty of Medicine.
Moriyoshi
K
K
Utsumi
T
T
Nakanishi
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002148:Calmodulin-Binding Proteins; D002417:Cattle; D015870:Gene Expression / Q000235:genetics; D008969:Molecular Sequence Data; D011506:Proteins / Q000235:genetics*
D002148:Calmodulin-Binding Proteins; D011506:Proteins