Biology:BOP1
 Generic protein structure example |
Ribosome biogenesis protein BOP1 is a protein that in humans is encoded by the BOP1 gene.[1][2] 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.
Function
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 mammalian cells.[6] In Giardia, the species specific cytoskeleton protein, beta-giardin, interacts with Bop1.[3]
Structure
| BOP1NT | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | BOP1NT | ||||||||
| Pfam | PF08145 | ||||||||
| InterPro | IPR012953 | ||||||||
| |||||||||
BOP1 contains a conserved N-terminal domain, BOP1NT.
References
- ↑ "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. Mar 1996. doi:10.1093/dnares/2.4.167. PMID 8590280.
- ↑ "Entrez Gene: BOP1 block of proliferation 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23246.
- ↑ 3.0 3.1 "Interaction of beta-giardin with the Bop1 protein in Giardia lamblia". Parasitol. Res. 98 (2): 138–44. January 2006. doi:10.1007/s00436-005-0040-8. PMID 16362343.
- ↑ "Contribution of the BOP1 gene, located on 8q24, to colorectal tumorigenesis". Genes Chromosomes Cancer 45 (9): 874–81. September 2006. doi:10.1002/gcc.20351. PMID 16804918.
- ↑ "Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization and assembly of the PeBoW complex required for maturation of the 60S ribosomal subunit". Mol. Cell. Biol. 27 (10): 3682–94. May 2007. doi:10.1128/MCB.00172-07. PMID 17353269.
- ↑ "Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required for ribosome biogenesis and cell proliferation". J. Cell Biol. 170 (3): 367–78. August 2005. doi:10.1083/jcb.200501141. PMID 16043514.
External links
- Human BOP1 genome location and BOP1 gene details page in the UCSC Genome Browser.
Further reading
- "Structural organization and promoter analysis of murine heat shock transcription factor-1 gene.". J. Biol. Chem. 273 (49): 32514–21. 1999. doi:10.1074/jbc.273.49.32514. PMID 9829985.
- "Gene cloning of immunogenic antigens overexpressed in pancreatic cancer.". Biochem. Biophys. Res. Commun. 281 (4): 936–44. 2001. doi:10.1006/bbrc.2001.4377. PMID 11237751.
- "Evidence of p53-dependent cross-talk between ribosome biogenesis and the cell cycle: effects of nucleolar protein Bop1 on G(1)/S transition.". Mol. Cell. Biol. 21 (13): 4246–55. 2001. doi:10.1128/MCB.21.13.4246-4255.2001. PMID 11390653.
- "ERB1, the yeast homolog of mammalian Bop1, is an essential gene required for maturation of the 25S and 5.8S ribosomal RNAs.". Nucleic Acids Res. 29 (17): 3621–30. 2001. doi:10.1093/nar/29.17.3621. PMID 11522832.
- "Directed proteomic analysis of the human nucleolus.". Curr. Biol. 12 (1): 1–11. 2002. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- "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. 2002. doi:10.1074/jbc.M204381200. PMID 12048210.
- "Functional proteomic analysis of human nucleolus.". Mol. Biol. Cell 13 (11): 4100–9. 2003. doi:10.1091/mbc.E02-05-0271. PMID 12429849.
- "Physical and functional interaction between Pes1 and Bop1 in mammalian ribosome biogenesis.". Mol. Cell 15 (1): 17–29. 2004. doi:10.1016/j.molcel.2004.05.020. PMID 15225545.
- "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. 2005. doi:10.1038/nature03207. PMID 15635413. Bibcode: 2005Natur.433...77A.
- "Phosphoproteome analysis of the human mitotic spindle.". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. 2006. doi:10.1073/pnas.0507066103. PMID 16565220. Bibcode: 2006PNAS..103.5391N.
- "A probability-based approach for high-throughput protein phosphorylation analysis and site localization.". Nat. Biotechnol. 24 (10): 1285–92. 2006. doi:10.1038/nbt1240. PMID 16964243.
- "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. 2007. doi:10.1038/msb4100134. PMID 17353931.
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