RBBP7
Histone-binding protein RBBP7 is a protein that in humans is encoded by the RBBP7 gene.[5]
Function
This protein is a ubiquitously expressed nuclear protein and belongs to a highly conserved subfamily of WD-repeat proteins. It is found among several proteins that binds directly to retinoblastoma protein, which regulates cell proliferation. The encoded protein is found in many histone deacetylase complexes, including mSin3 co-repressor complex. It is also present in protein complexes involved in chromatin assembly. This protein can interact with BRCA1 tumor-suppressor gene and may have a role in the regulation of cell proliferation and differentiation.[6]
Model organisms
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Normal |
| Homozygous Fertility | Normal |
| Body weight | Normal |
| Anxiety | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Hot plate | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Normal |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Normal |
| Haematology | Normal |
| Peripheral blood lymphocytes | Abnormal[7] |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Brain histopathology | Normal |
| All tests and analysis from[8][9] |
Model organisms have been used in the study of RBBP7 function. A conditional knockout mouse line, called Rbbp7tm1a(EUCOMM)Wtsi[10][11] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[12][13][14]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[8][15] Twenty one tests were carried out on mutant mice and one significant abnormality was observed: hemizygous mutant males had decreased CD4-positive and CD8-positive T cell numbers.[8]
Interactions
RBBP7 has been shown to interact with:
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000102054 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031353 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b Qian YW, Lee EY (Dec 1995). "Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast". J Biol Chem. 270 (43): 25507–25513. doi:10.1074/jbc.270.43.25507. PMID 7503932.
- ^ "Entrez Gene: RBBP7 retinoblastoma binding protein 7".
- ^ "Peripheral blood lymphocytes data for Rbbp7". Wellcome Trust Sanger Institute.[dead link]
- ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
- ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ^ "International Knockout Mouse Consortium".
- ^ "Mouse Genome Informatics".
- ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
- ^ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
- ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ a b Yarden RI, Brody LC (April 1999). "BRCA1 interacts with components of the histone deacetylase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4983–8. doi:10.1073/pnas.96.9.4983. PMC 21803. PMID 10220405.
- ^ Chen GC, Guan LS, Yu JH, Li GC, Choi Kim HR, Wang ZY (June 2001). "Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1". Biochem. Biophys. Res. Commun. 284 (2): 507–14. doi:10.1006/bbrc.2001.5003. PMID 11394910.
- ^ Yarden RI, Brody LC (2001). "Identification of proteins that interact with BRCA1 by Far-Western library screening" (Submitted manuscript). J. Cell. Biochem. 83 (4): 521–31. doi:10.1002/jcb.1257. PMID 11746496.
- ^ Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y (January 2002). "Identification and functional characterization of the p66/p68 components of the MeCP1 complex". Mol. Cell. Biol. 22 (2): 536–46. doi:10.1128/mcb.22.2.536-546.2002. PMC 139742. PMID 11756549.
- ^ a b Yao YL, Yang WM (October 2003). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". J. Biol. Chem. 278 (43): 42560–8. doi:10.1074/jbc.M302955200. PMID 12920132.
- ^ Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A (September 1999). "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex". Nat. Genet. 23 (1): 58–61. doi:10.1038/12659. hdl:1842/684. PMID 10471499.
- ^ a b c Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (August 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
- ^ Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–64. doi:10.1016/s0092-8674(00)80216-0. PMID 9150135.
- ^ a b Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (June 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell. 1 (7): 1021–31. doi:10.1016/s1097-2765(00)80102-1. PMID 9651585.
- ^ a b Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (February 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Mol. Cell. Biol. 22 (3): 835–48. doi:10.1128/mcb.22.3.835-848.2002. PMC 133546. PMID 11784859.
Further reading
- Huang S, Lee WH, Lee EY (1991). "A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product". Nature. 350 (6314): 160–162. doi:10.1038/350160a0. PMID 2005966.
- Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–364. doi:10.1016/S0092-8674(00)80216-0. PMID 9150135.
- Verreault A, Kaufman PD, Kobayashi R, Stillman B (1998). "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase". Curr. Biol. 8 (2): 96–108. doi:10.1016/S0960-9822(98)70040-5. PMID 9427644.
- Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell. 1 (7): 1021–1031. doi:10.1016/S1097-2765(00)80102-1. PMID 9651585.
- Guan LS, Rauchman M, Wang ZY (1998). "Induction of Rb-associated protein (RbAp46) by Wilms' tumor suppressor WT1 mediates growth inhibition". J. Biol. Chem. 273 (42): 27047–27050. doi:10.1074/jbc.273.42.27047. PMID 9765217.
- Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (1998). "The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities". Cell. 95 (2): 279–289. doi:10.1016/S0092-8674(00)81758-4. PMID 9790534.
- Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature. 395 (6705): 917–921. doi:10.1038/27699. PMID 9804427.
- Yarden RI, Brody LC (1999). "BRCA1 interacts with components of the histone deacetylase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4983–4988. doi:10.1073/pnas.96.9.4983. PMC 21803. PMID 10220405.
- Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15): 1924–1935. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
- Wade PA, Gegonne A, Jones PL, Ballestar E, Aubry F, Wolffe AP (1999). "Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation". Nat. Genet. 23 (1): 62–66. doi:10.1038/12664. PMID 10471500.
- Zhang Q, Vo N, Goodman RH (2000). "Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB". Mol. Cell. Biol. 20 (14): 4970–4978. doi:10.1128/MCB.20.14.4970-4978.2000. PMC 85947. PMID 10866654.
- Humphrey GW, Wang Y, Russanova VR, Hirai T, Qin J, Nakatani Y, Howard BH (2001). "Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1". J. Biol. Chem. 276 (9): 6817–6824. doi:10.1074/jbc.M007372200. PMID 11102443.
- Skowyra D, Zeremski M, Neznanov N, Li M, Choi Y, Uesugi M, Hauser CA, Gu W, Gudkov AV, Qin J (2001). "Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex". J. Biol. Chem. 276 (12): 8734–8739. doi:10.1074/jbc.M007664200. PMID 11118440.
- Chen GC, Guan LS, Yu JH, Li GC, Choi Kim HR, Wang ZY (2001). "Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1". Biochem. Biophys. Res. Commun. 284 (2): 507–514. doi:10.1006/bbrc.2001.5003. PMID 11394910.
- Yarden RI, Brody LC (2002). "Identification of proteins that interact with BRCA1 by Far-Western library screening" (Submitted manuscript). J. Cell. Biochem. 83 (4): 521–531. doi:10.1002/jcb.1257. PMID 11746496.
- Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Mol. Cell. Biol. 22 (3): 835–848. doi:10.1128/MCB.22.3.835-848.2002. PMC 133546. PMID 11784859.
- Vaute O, Nicolas E, Vandel L, Trouche D (2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. 30 (2): 475–481. doi:10.1093/nar/30.2.475. PMC 99834. PMID 11788710.
- Saito M, Ishikawa F (2002). "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2". J. Biol. Chem. 277 (38): 35434–35439. doi:10.1074/jbc.M203455200. PMID 12124384.
- Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D (2002). "Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein". Genes Dev. 16 (22): 2893–2905. doi:10.1101/gad.1035902. PMC 187479. PMID 12435631.