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SMUG1
Introduction
Single-strand-selective monofunctional uracil-DNA glycosylase 1, also known as SMUG1, is a human gene.[1]
SMUG1 is a glycosylase that removes uracil from single- and double-stranded DNA in nuclear chromatin, thus contributing to base excision repair.[supplied by OMIM][1]
References
References
Further reading
Further reading
- Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1–2): 171–4. PMID 8125298.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1–2): 149–56. PMID 9373149.
- Haushalter KA, Todd Stukenberg MW, Kirschner MW, Verdine GL (1999). “Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors”. Curr. Biol. 9 (4): 174–85. PMID 10074426.
- Boorstein RJ, Cummings A, Marenstein DR; et al. (2001). “Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1”. J. Biol. Chem. 276 (45): 41991–7. doi:10.1074/jbc.M106953200. PMID 11526119.
- Kavli B, Sundheim O, Akbari M; et al. (2002). “hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup”. J. Biol. Chem. 277 (42): 39926–36. doi:10.1074/jbc.M207107200. PMID 12161446.
- 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. PMID 12477932.
- Masaoka A, Matsubara M, Hasegawa R; et al. (2003). “Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions”. Biochemistry. 42 (17): 5003–12. doi:10.1021/bi0273213. PMID 12718543.
- Wibley JE, Waters TR, Haushalter K; et al. (2003). “Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1”. Mol. Cell. 11 (6): 1647–59. PMID 12820976.
- Ota T, Suzuki Y, Nishikawa T; et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Matsubara M, Tanaka T, Terato H; et al. (2004). “Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase”. Nucleic Acids Res. 32 (17): 5291–302. doi:10.1093/nar/gkh859. PMID 15466595.
- Gerhard DS, Wagner L, Feingold EA; et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
- Schröfelbauer B, Yu Q, Zeitlin SG, Landau NR (2005). “Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases”. J. Virol. 79 (17): 10978–87. doi:10.1128/JVI.79.17.10978-10987.2005. PMID 16103149.
- Rual JF, Venkatesan K, Hao T; et al. (2005). “Towards a proteome-scale map of the human protein-protein interaction network”. Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Di Noia JM, Rada C, Neuberger MS (2006). “SMUG1 is able to excise uracil from immunoglobulin genes: insight into mutation versus repair”. EMBO J. 25 (3): 585–95. doi:10.1038/sj.emboj.7600939. PMID 16407970.
- Broderick P, Bagratuni T, Vijayakrishnan J; et al. (2006). “Evaluation of NTHL1, NEIL1, NEIL2, MPG, TDG, UNG and SMUG1 genes in familial colorectal cancer predisposition”. BMC Cancer. 6: 243. doi:10.1186/1471-2407-6-243. PMIDÂ 17029639.
- Matsubara M, Tanaka T, Terato H, Ide H (2007). “Action mechanism of human SMUG1 uracil-DNA glycosylase”. Nucleic Acids Symp Ser (Oxf) (49): 295–6. doi:10.1093/nass/49.1.295. PMID 17150750.
- Pettersen HS, Sundheim O, Gilljam KM; et al. (2007). “Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms”. Nucleic Acids Res. 35 (12): 3879–92. doi:10.1093/nar/gkm372. PMID 17537817.
