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(Received for publication, May 8, 1996, and in revised form, July 26, 1996)
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.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27855-27862
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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