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Volume 271, Number 44, Issue of November 1, 1996 pp. 27855-27862
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Distinct Troponin T Genes Are Expressed in Embryonic/Larval Tail Striated Muscle and Adult Body Wall Smooth Muscle of Ascidian

(Received for publication, May 8, 1996, and in revised form, July 26, 1996)

Takeshi Endo , Ken Matsumoto , Taro Hama , Yukio Ohtsuka , Go Katsura and Takashi Obinata

From the Department of Biology, Faculty of Science, Chiba University, Yayoicho, Inageku, Chiba 263, Japan

During development of the ascidian Halocynthia roretzi, the tadpole larva hatched from the tailbud embryo metamorphoses to the sessile adult with a body wall muscle. Although the adult body wall muscle is morphologically nonsarcomeric smooth muscle, it contains troponin complex consisting of three subunits (T, I, and C) as do vertebrate striated muscles. Different from vertebrate troponins, however, the smooth muscle troponin promotes actomyosin Mg2+-ATPase activity in the presence of high concentration of Ca2+, and this promoting property is attributable to troponin T. To address whether the embryonic/larval tail striated muscle and the adult smooth muscle utilize identical or different regulatory machinery, we cloned troponin T cDNAs from each cDNA library. The embryonic and the adult troponin Ts were encoded by distinct genes and shared only <60% identity with each other. Northern blotting and whole mount in situ hybridization revealed that these isoforms were specifically expressed in the embryonic/larval tail striated muscle and the adult smooth muscle, respectively. These results may imply that these isoforms regulate actin-myosin interaction in different manners. The adult troponin T under forced expression in mouse fibroblasts was unexpectedly located in the nuclei. However, a truncated protein with a deletion including a cluster of basic amino acids colocalized with tropomyosin on actin filaments. Thus, complex formation with troponin I and C immediately after the synthesis is likely to be essential for the protein to properly localize on the thin filaments.


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