ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity

作者: Tomohiko Ohta , Jennifer J. Michel , Arndt J. Schottelius , Yue Xiong

DOI: 10.1016/S1097-2765(00)80482-7

关键词:

摘要: We have identified two highly conserved RING finger proteins, ROC1 and ROC2, that are homologous to APC11, a subunit of the anaphase-promoting complex. ROC2 commonly interact with all cullins while APC11 specifically interacts APC2, cullin-related APC subunit. YeastROC1 encodes an essential gene whose reduced expression resulted in multiple, elongated buds accumulation Sic1p Cln2p. immunocomplexes can catalyze isopeptide ligations form polyubiquitin chains E1- E2-dependent manner. mutations completely abolished their ligase activity without noticeable changes associated proteins. Ubiquitination phosphorylated I kappa B alpha be catalyzed by immunocomplex vitro. Hence, combinations ROC/APC11 cullin proteins potentially constitute wide variety ubiquitin ligases.

参考文章(23)
Christopher W. Jenkins, Yue Xiong, Immunoprecipitation and Immunoblotting in Cell Cycle Studies Springer, Berlin, Heidelberg. pp. 250- 263 ,(1996) , 10.1007/978-3-642-57783-3_22
J.R. Lamb, W.A. Michaud, R.S. Sikorski, P.A. Hieter, Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis. The EMBO Journal. ,vol. 13, pp. 4321- 4328 ,(1994) , 10.1002/J.1460-2075.1994.TB06752.X
A Hershko, H Heller, S Elias, A Ciechanover, Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. Journal of Biological Chemistry. ,vol. 258, pp. 8206- 8214 ,(1983) , 10.1016/S0021-9258(20)82050-X
J R Pringle, B Byers, M G Goebl, N Mathias, S L Johnson, M Winey, A E Adams, L Goetsch, CDC53P ACTS IN CONCERT WITH CDC4P AND CDC34P TO CONTROL THE G1-TO-S-PHASE TRANSITION AND IDENTIFIES A CONSERVED FAMILY OF PROTEINS Molecular and Cellular Biology. ,vol. 16, pp. 6634- 6643 ,(1996) , 10.1128/MCB.16.12.6634
PAUL S. FREEMONT, The RING finger. A novel protein sequence motif related to the zinc finger. Annals of the New York Academy of Sciences. ,vol. 684, pp. 174- 192 ,(1993) , 10.1111/J.1749-6632.1993.TB32280.X
J. T. Winston, P. Strack, P. Beer-Romero, C. Y. Chu, S. J. Elledge, J. W. Harper, The SCFβ-TRCP–ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro Genes & Development. ,vol. 13, pp. 270- 283 ,(1999) , 10.1101/GAD.13.3.270
R.M.Renny Feldman, Craig C Correll, Kenneth B Kaplan, Raymond J Deshaies, A Complex of Cdc4p, Skp1p, and Cdc53p/Cullin Catalyzes Ubiquitination of the Phosphorylated CDK Inhibitor Sic1p Cell. ,vol. 91, pp. 221- 230 ,(1997) , 10.1016/S0092-8674(00)80404-3
Mark S. Longtine, Amos Mckenzie III, Douglas J. Demarini, Nirav G. Shah, Achim Wach, Arndt Brachat, Peter Philippsen, John R. Pringle, Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae Yeast. ,vol. 14, pp. 953- 961 ,(1998) , 10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U
Michael Glotzer, Andrew W. Murray, Marc W. Kirschner, Cyclin is degraded by the ubiquitin pathway Nature. ,vol. 349, pp. 132- 138 ,(1991) , 10.1038/349132A0
Randall W King, Jan-Michael Peters, Stuart Tugendreich, Mark Rolfe, Philip Hieter, Marc W Kirschner, A 20s complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B Cell. ,vol. 81, pp. 279- 288 ,(1995) , 10.1016/0092-8674(95)90338-0