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J Biol Chem, Vol. 274, Issue 52, 37070-37078, December 24, 1999
Cytosolic Chaperonin Is Up-regulated during Cell Growth
PREFERENTIAL EXPRESSION AND BINDING TO TUBULIN AT
G1/S TRANSITION THROUGH EARLY S PHASE*
Shin-ichi
Yokota,
Hideki
Yanagi,
Takashi
Yura, and
Hiroshi
Kubota
From the HSP Research Institute, Kyoto Research Park, 17 Chudoji
Minami-machi, Shimogyo-ku, Kyoto 600-8813, Japan
The chaperonin containing t-complex
polypeptide 1 (CCT) is a heterooligomeric molecular chaperone assisting
in the folding of actin, tubulin, and other cytosolic proteins. The
expression levels of CCT subunits varied among seven mouse cell lines
tested but showed a close correlation with growth rate. Both the CCT protein and mRNA levels in the human promyelolytic cell HL60
decreased concomitant with growth arrest during differentiation. More
rapid decrease in CCT level occurred when the mouse interleukin
(IL)-3-dependent myeloid DA3 cells were starved for IL-3.
Readdition of IL-3 caused rapid resumption of CCT synthesis during
synchronous growth: the maximum CCT protein and mRNA levels were
observed at G1/S transition through early S phase. The
turnover rate of CCT was nearly constant regardless of growth. Gel
filtration and immunoprecipitation analyses indicated that CCT in
vivo is associated with tubulin at early S phase, but not at
G0/G1 phase. These results demonstrated that CCT expression is strongly up-regulated during cell growth especially from G1/S transition to early S phase and is primarily
controlled at the mRNA level. CCT appears to play important roles
for cell growth by assisting in the folding of tubulin and other proteins.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 81-75-315-8656;
Fax: 81-75-315-8659; E-mail: kubota@hsp.co.jp.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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