This entry includes proteins with a JmjC domain that belong to the cupin superfamily, including Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 [1], Ribosomal oxygenase 1/2 [2,3], and 50S ribosomal protein L16 3-hydroxylase from Escherichia coli [4,5]. Proteins are bifunctional, acting as histone lysine demethylases and ribosomal histidine hydroxylases. [1]. 20057358. SLR-2 and JMJC-1 regulate an evolutionarily conserved stress-response network. Kirienko NV, Fay DS;. EMBO J. 2010;29:727-739. [2]. 23103944. Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans. Ge W, Wolf A, Feng T, Ho CH, Sekirnik R, Zayer A, Granatino N, Cockman ME, Loenarz C, Loik ND, Hardy AP, Claridge TDW, Hamed RB, Chowdhury R, Gong L, Robinson CV, Trudgian DC, Jiang M, Mackeen MM, Mccullagh JS, Gordiyenko Y, Thalhammer A, Yamamoto A, Yang M, Liu-Yi P, Zhang Z, Schmidt-Zachmann M, Kessler BM, Ratcliffe PJ, Preston GM, Coleman ML, Schofield CJ;. Nat Chem Biol. 2012;8:960-962. [3]. 19502796. Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3. Lu Y, Chang Q, Zhang Y, Beezhold K, Rojanasakul Y, Zhao H, Castranova V, Shi X, Chen F;. Cell Cycle. 2009;8:2101-2109. [4]. 24530688. Structure and functional analysis of YcfD, a novel 2-oxoglutarate/Fe(2)(+)-dependent oxygenase involved in translational regulation in Escherichia coli. van Staalduinen LM, Novakowski SK, Jia Z;. J Mol Biol. 2014;426:1898-1910. [5]. 24814345. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Chowdhury R, Sekirnik R, Brissett NC, Krojer T, Ho CH, Ng SS, Clifto. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16