TY - JOUR
T1 - Tetrahymena elongation factor-1α is localized with calmodulin in the division furrow
AU - Numata, Osamu
AU - Kurasawa, Yasuhiro
AU - Gonda, Kohsuke
AU - Watanabe, Yoshio
PY - 2000
Y1 - 2000
N2 - Translation elongation factor 1α (EF-1α) catalyzes the GTP-dependent binding of aminoacyl-tRNA to ribosomes. We previously reported that Tetrahymena EF-1α induced the formation of bundles of rabbit skeletal muscle filamentous actin (F-actin) as well as Tetrahymena F-actin [Kurasawa et al. (1996) Zool. Sci. (Tokyo) 13, 371-375], and that Ca2+/calmodulin (CAM) regulated the F-actin-bundling activity of EF-1α [Kurasawa et al. (1996) J. Biochem. 119, 791-798]. In the present study, we investigated the binding between Tetrahymena EF-1α and CaM using a Tetrahymena EF-1α affinity column, and the localization of EF-1α and CaM by indirect immunofluorescence. Only CaM in the Tetrahymena cell extract bound to Tetrahymena EF-1α in a Ca2+-dependent manner. In interphase Tetrahymena cells, EF-1α and CaM are colocalized in the crescent structure of the oral apparatus and the apical ring, while in dividing cells, they are colocalized in the division furrow. This is the first report describing the coexistence of EF-1α and CaM in the division furrow, suggesting that EF-1α and CaM are involved in the organization of contractile ring microfilaments during cytokinesis.
AB - Translation elongation factor 1α (EF-1α) catalyzes the GTP-dependent binding of aminoacyl-tRNA to ribosomes. We previously reported that Tetrahymena EF-1α induced the formation of bundles of rabbit skeletal muscle filamentous actin (F-actin) as well as Tetrahymena F-actin [Kurasawa et al. (1996) Zool. Sci. (Tokyo) 13, 371-375], and that Ca2+/calmodulin (CAM) regulated the F-actin-bundling activity of EF-1α [Kurasawa et al. (1996) J. Biochem. 119, 791-798]. In the present study, we investigated the binding between Tetrahymena EF-1α and CaM using a Tetrahymena EF-1α affinity column, and the localization of EF-1α and CaM by indirect immunofluorescence. Only CaM in the Tetrahymena cell extract bound to Tetrahymena EF-1α in a Ca2+-dependent manner. In interphase Tetrahymena cells, EF-1α and CaM are colocalized in the crescent structure of the oral apparatus and the apical ring, while in dividing cells, they are colocalized in the division furrow. This is the first report describing the coexistence of EF-1α and CaM in the division furrow, suggesting that EF-1α and CaM are involved in the organization of contractile ring microfilaments during cytokinesis.
KW - Actin
KW - Calmodulin
KW - Cytokinesis
KW - Elongation factor 1α (EF-1α)
KW - Tetrahymena
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U2 - 10.1093/oxfordjournals.jbchem.a022583
DO - 10.1093/oxfordjournals.jbchem.a022583
M3 - Article
C2 - 10731666
AN - SCOPUS:0033965227
VL - 127
SP - 51
EP - 56
JO - Journal of Biochemistry
JF - Journal of Biochemistry
SN - 0021-924X
IS - 1
ER -