Journal Article

Cloning and Sequencing of the Gene for a <i>Tetrahymena</i> Fimbrin-Like Protein

Atsushi Watanabe, Izuru Yonemura, Kohsuke Gonda and Osamu Numata

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 127, issue 1, pages 85-94
Published in print January 2000 | ISSN: 0021-924X
Published online January 2000 | e-ISSN: 1756-2651 | DOI: https://dx.doi.org/10.1093/oxfordjournals.jbchem.a022587
Cloning and Sequencing of the Gene for a Tetrahymena Fimbrin-Like Protein

Show Summary Details

Preview

Tetrahymena F-actin-binding protein, which induces bundling of Tetrahymena F-actin, was localized to a division furrow during cytokinesis. We report here the cloning and characterization of the gene and cDNA of a Tetrahymena F-actin-binding protein. The cDNA encodes a protein comprising 579 deduced amino acids with a calculated molecular mass of 65.9 kDa. The predicted amino acid sequence shares 37.7, 41.8, and 39% identity with the sequences of yeast fimbrin, Arabidopsis thaliana fimbrin, and Dictyo-stelium discoideum plastin, respectively. The Tetrahymena F-actin-binding protein also shares two actin-binding domains previously identified in the fimbrin/plastin family, but lacks the EF-hand Ca2+-binding motif, suggesting that this protein is a novel-fimbrin-like protein in Tetrahymena. Moreover, we cloned a genomic DNA encoding the Tetrahymena fimbrin-like protein and performed Southern and Northern hybridizations. The results indicate that the genomic DNA possesses 9 introns and that both the gene and transcript of Tetrahymena fimbrin-like protein are single. Thus, we suggest that Tetrahymena fimbrin-like protein localizes to the division furrow and probably cross-links actin filaments in a Ca2+-insensitive manner during cytokinesis.

Keywords: cytokinesis; F-actin bundling; fimbrin/plastin family; RACE; Tetrahymena

Journal Article.  0 words. 

Subjects: Biochemistry

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.