It is a WD40 repeat-containing nucleolar protein involved in rRNA processing, thereby controlling the cell cycle.[3] It is required for the maturation of the 25S and 5.8S ribosomal RNAs. It may serve as an essential factor in ribosome formation that coordinates processing of the spacer regions in pre-rRNA. The Pes1-Bop1 complex has several components: BOP1, GRWD1, PES1, ORC6L, and RPL3 and is involved in ribosome biogenesis and altered chromosome segregation. The overexpression of BOP1 increases the percentage of multipolar spindles in human cells. Deregulation of the BOP1 pathway may contribute to colorectal tumourigenesis in humans.[4] Elevated levels of Bop1 induces Bop1/WDR12 and Bop1/Pes1 subcomplexes and the assembly and integrity of the PeBoW complex is highly sensitive to changes in Bop1 protein levels.[5]
Nop7p-Erb1p-Ytm1p, found in yeast, is potentially the homologous complex of Pes1-Bop1-WDR12 as it is involved in the control of ribosome biogenesis and S phase entry. The integrity of the PeBoW complex is required for ribosome biogenesis and cell proliferation in mammaliancells.[6] In Giardia, the species specific cytoskeleton protein, beta-giardin, interacts with Bop1.[3]
BOP1 contains a conserved N-terminal domain, BOP1NT.
References
↑Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N (Mar 1996). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res. 2 (4): 167–74, 199–210. doi:10.1093/dnares/2.4.167. PMID8590280.
↑ 3.03.1Kim J, Goo SY, Chung HJ, Yang HW, Yong TS, Lee KH, Park SJ (January 2006). "Interaction of beta-giardin with the Bop1 protein in Giardia lamblia". Parasitol. Res. 98 (2): 138–44. doi:10.1007/s00436-005-0040-8. PMID16362343.
↑Killian A, Sarafan-Vasseur N, Sesboüé R, Le Pessot F, Blanchard F, Lamy A, Laurent M, Flaman JM, Frébourg T (September 2006). "Contribution of the BOP1 gene, located on 8q24, to colorectal tumorigenesis". Genes Chromosomes Cancer. 45 (9): 874–81. doi:10.1002/gcc.20351. PMID16804918.
Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID11790298.
Strezoska Z, Pestov DG, Lau LF (2002). "Functional inactivation of the mouse nucleolar protein Bop1 inhibits multiple steps in pre-rRNA processing and blocks cell cycle progression". J. Biol. Chem. 277 (33): 29617–25. doi:10.1074/jbc.M204381200. PMID12048210.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID16964243.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID17081983.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC1847948. PMID17353931.
