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Titolo:
Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle
Autore:
Yokota, S; Yanagi, H; Yura, T; Kubota, H;
Indirizzi:
Kyoto Univ, Inst Frontier Med Sci, Dept Mol & Cellular Biol, Sakyo Ku, Kyoto 6068397, Japan Kyoto Univ Kyoto Japan 6068397 ular Biol, Sakyo Ku, Kyoto 6068397, Japan HSP Res Inst, Shimogyo Ku, Kyoto, Japan HSP Res Inst Kyoto JapanHSP Res Inst, Shimogyo Ku, Kyoto, Japan JST, CREST, Tsukuba, Ibaraki, Japan JST Tsukuba Ibaraki JapanJST, CREST, Tsukuba, Ibaraki, Japan
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 17, volume: 268, anno: 2001,
pagine: 4664 - 4673
SICI:
0014-2956(200109)268:17<4664:CCTP1C>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYTOPLASMIC CHAPERONIN; IN-VIVO; EUKARYOTIC CYTOSOL; CONTAINING TCP-1; CCT CHAPERONIN; BETA-ACTIN; SACCHAROMYCES-CEREVISIAE; MOLECULAR CHAPERONES; PROTEIN; TUBULIN;
Keywords:
CCT; cell cycle; molecular chaperone; protein folding; subunit content;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Kubota, H Kyoto Univ, Inst Frontier Med Sci, Dept Mol & Cellular Biol, Sakyo Ku, 53 Shogoin Kawahara Cho, Kyoto 6068397, Japan Kyoto Univ 53 Shogoin Kawahara Cho Kyoto Japan 6068397 7, Japan
Citazione:
S. Yokota et al., "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle", EUR J BIOCH, 268(17), 2001, pp. 4664-4673

Abstract

The chaperonin-containing t-complex polypeptide 1 (CCT) is a cytosolic molecular chaperone composed of eight subunits that assists in the folding of actin, tubulin and other cytosolic proteins. We show here that the content of particular subunits of CCT within mammalian cells decreases concomitantly with the reduction of chaperone activity during cell cycle arrest at M phase. CCT recovers chaperone activity upon resumption of these subunits after release from M phase arrest or during arrest at S phase. The levels of alpha, delta and zeta -1 subunits decreased more rapidly than the other subunits during M phase arrest by colcemid treatment and recovered after releasefrom the arrest. Gel filtration chromatography or native (nondenaturing) PAGE analysis followed by immunoblotting indicated that the alpha and delta subunit content in the 700- to 900-kDa CCT complex was appreciably lower inthe M phase cells than in asynchronous cells. In vivo, the CCT complex of M-phase-arrested cells was found to bind lower amounts of tubulin than thatof asynchronous cells. In vitro, the CCT complex of M phase-arrested cellswas less active in binding and folding denatured actin than that of asynchronous cells. On the other hand, the CCT complex of asynchronous cells (a mixture of various phases of cell cycle) exhibited lower alpha and delta subunit content and lower chaperone activity than that of S-phase-arrested cells obtained by excess thymidine treatment. In addition, turnover (synthesisand degradation) rates of the alpha and delta subunits in vivo were more rapid than those of most other subunits. These results suggest that the content of alpha and delta subunits of CCT reduces from the complete active complex in S phase cells to incomplete inactive complex in M phase cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 21:13:32