RDBP
Negative elongation factor E is a protein that in humans is encoded by the RDBP gene.[1]
The protein encoded by this gene is part of a complex termed negative elongation factor (NELF) which represses RNA polymerase II transcript elongation. This protein bears similarity to nuclear RNA-binding proteins; however, it has not been demonstrated that this protein binds RNA. The protein contains a tract of alternating basic and acidic residues, largely arginine (R) and aspartic acid (D). The gene localizes to the major histocompatibility complex (MHC) class III region on chromosome 6.[1]
Interactions
RDBP has been shown to interact with TH1L,[2][3] WHSC2[3] and Cofactor of BRCA1.[4][3]
References
- ^ a b "Entrez Gene: RDBP RD RNA binding protein". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7936.
- ^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.
- ^ a b c Narita, Takashi; Yamaguchi Yuki, Yano Keiichi, Sugimoto Seiji, Chanarat Sittinan, Wada Tadashi, Kim Dong-ki, Hasegawa Jun, Omori Masashi, Inukai Naoto, Endoh Masaki, Yamada Tomoko, Handa Hiroshi (Mar. 2003). "Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex". Mol. Cell. Biol. (United States) 23 (6): 1863–73. doi:10.1128/MCB.23.6.1863-1873.2003. ISSN 0270-7306. PMC 149481. PMID 12612062. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=149481.
- ^ Lehner, Ben; Semple Jennifer I, Brown Stephanie E, Counsell Damian, Campbell R Duncan, Sanderson Christopher M (Jan. 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics (United States) 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. ISSN 0888-7543. PMID 14667819.
Further reading
- Yu CY (1999). "Molecular genetics of the human MHC complement gene cluster.". Exp. Clin. Immunogenet. 15 (4): 213–30. doi:10.1159/000019075. PMID 10072631.
- Stevens M, De Clercq E, Balzarini J (2007). "The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention.". Med Res Rev 26 (5): 595–625. doi:10.1002/med.20081. PMID 16838299.
- Surowy CS, Hoganson G, Gosink J, et al. (1990). "The human RD protein is closely related to nuclear RNA-binding proteins and has been highly conserved.". Gene 90 (2): 299–302. doi:10.1016/0378-1119(90)90194-V. PMID 2119325.
- Speiser PW, White PC (1990). "Structure of the human RD gene: a highly conserved gene in the class III region of the major histocompatibility complex.". DNA 8 (10): 745–51. doi:10.1089/dna.1989.8.745. PMID 2612324.
- Lévi-Strauss M, Carroll MC, Steinmetz M, Meo T (1988). "A previously undetected MHC gene with an unusual periodic structure.". Science 240 (4849): 201–4. doi:10.1126/science.3353717. PMID 3353717.
- Cheng J, Macon KJ, Volanakis JE (1993). "cDNA cloning and characterization of the protein encoded by RD, a gene located in the class III region of the human major histocompatibility complex.". Biochem. J. 294 ( Pt 2): 589–93. PMC 1134496. PMID 8373374. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1134496.
- Lee SG, Song K (1997). "Genomic organization of the human DDX13 gene located between RD and RP1 in the class III MHC complex.". Mol. Cells 7 (3): 414–8. PMID 9264031.
- Büssow K, Cahill D, Nietfeld W, et al. (1998). "A method for global protein expression and antibody screening on high-density filters of an arrayed cDNA library.". Nucleic Acids Res. 26 (21): 5007–8. doi:10.1093/nar/26.21.5007. PMC 147919. PMID 9776767. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=147919.
- Yang Z, Shen L, Dangel AW, et al. (1998). "Four ubiquitously expressed genes, RD (D6S45)-SKI2W (SKIV2L)-DOM3Z-RP1 (D6S60E), are present between complement component genes factor B and C4 in the class III region of the HLA.". Genomics 53 (3): 338–47. doi:10.1006/geno.1998.5499. PMID 9799600.
- Yamaguchi Y, Takagi T, Wada T, et al. (1999). "NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation.". Cell 97 (1): 41–51. doi:10.1016/S0092-8674(00)80713-8. PMID 10199401.
- Ping YH, Rana TM (2001). "DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation.". J. Biol. Chem. 276 (16): 12951–8. doi:10.1074/jbc.M006130200. PMID 11112772.
- Yamaguchi Y, Inukai N, Narita T, et al. (2002). "Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA.". Mol. Cell. Biol. 22 (9): 2918–27. doi:10.1128/MCB.22.9.2918-2927.2002. PMC 133766. PMID 11940650. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133766.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Narita T, Yamaguchi Y, Yano K, et al. (2003). "Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex.". Mol. Cell. Biol. 23 (6): 1863–73. doi:10.1128/MCB.23.6.1863-1873.2003. PMC 149481. PMID 12612062. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=149481.
- Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
- Xie T, Rowen L, Aguado B, et al. (2004). "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.". Genome Res. 13 (12): 2621–36. doi:10.1101/gr.1736803. PMC 403804. PMID 14656967. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=403804.
- Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region.". Genomics 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
- Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446.
- Aiyar SE, Sun JL, Blair AL, et al. (2004). "Attenuation of estrogen receptor alpha-mediated transcription through estrogen-stimulated recruitment of a negative elongation factor.". Genes Dev. 18 (17): 2134–46. doi:10.1101/gad.1214104. PMC 515291. PMID 15342491. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=515291.
External links
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PDB gallery
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1x5p: Solution structure of RRM domain in Parp14
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2bz2: SOLUTION STRUCTURE OF NELF E RRM
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