title: Destrin, a mammalian actin-depolymerizing protein, is closely related to cofilin. Cloning and expression of porcine brain destrin cDNA.
abstract: Destrin is a mammalian 19-kDa protein that rapidly depolymerizes F-actin in a stoichiometric manner. In this study, we isolated cDNA clones coding for destrin from a porcine brain cDNA library. The deduced amino acid sequence of destrin is 165 residues long and is very similar (71% identical) to that of cofilin, a widely distributed, pH-sensitive actin-modulating protein. Destrin contains a sequence nearly identical with the putative nuclear transport signal sequence of cofilin and a hexapeptide sequence identical with the amino-terminal sequence (residues 2-7) of tropomyosin, which is shown to be involved in cofilin binding to actin. Destrin, like cofilin, also has in its carboxyl-terminal portion a region homologous to the sequence shared by gelsolin, fragmin, and Acanthamoeba profilin. We have expressed destrin as well as cofilin in Escherichia coli, purified them, and examined their function in vitro. The two proteins were found to differ in their interaction with actin, like destrin and cofilin isolated from porcine brain. This suggests that the difference in the function of the two proteins results from the subtle difference in their amino acid sequence rather than possible differences in post-translational modifications. Northern blot analyses indicated that both destrin mRNA and cofilin mRNA are widely distributed in various tissues, but both mRNAs differ in their relative abundance among tissues.
authors.affiliation: Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Moriyama
authors.forename: E
authors.initials: E
authors.lastname: Nishida
authors.forename: N
authors.initials: N
authors.lastname: Yonezawa
authors.forename: H
authors.initials: H
authors.lastname: Sakai
authors.forename: S
authors.initials: S
authors.lastname: Matsumoto
authors.forename: K
authors.initials: K
authors.lastname: Iida
authors.forename: I
authors.initials: I
authors.lastname: Yahara
mesh_terms: D000048:Acanthamoeba / Q000032:analysis; D051339:Actin Depolymerizing Factors; D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001923:Brain Chemistry; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D003285:Contractile Proteins; D003598:Cytoskeletal Proteins; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D051345:Destrin; D004926:Escherichia coli; D018260:Gelsolin; D015870:Gene Expression; D006495:Heparin, Low-Molecular-Weight; D051379:Mice; D008840:Microfilament Proteins; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000235:genetics; D051304:Profilins; D012333:RNA, Messenger / Q000032:analysis; D011994:Recombinant Proteins; D012689:Sequence Homology, Nucleic Acid; D013552:Swine; D014018:Tissue Distribution; D014335:Tropomyosin
chemical_list: D051339:Actin Depolymerizing Factors; D000199:Actins; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D003285:Contractile Proteins; D003598:Cytoskeletal Proteins; D051345:Destrin; C495825:Dstn protein, mouse; D018260:Gelsolin; D006495:Heparin, Low-Molecular-Weight; D008840:Microfilament Proteins; D009419:Nerve Tissue Proteins; C495739:Pfn1 protein, mouse; D051304:Profilins; D012333:RNA, Messenger; D011994:Recombinant Proteins; D014335:Tropomyosin; D004247:DNA