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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

  作者 GE WEI; WOLF ALEXANDER; FENG TIANSHU; HO CHIAHUA; SEKIRNIK ROK; ZAYER ADAM; GRANATINO NICOLAS; COCKMAN MATTHEW E; LOENARZ CHRISTOPH; LOIK NIKITA D; HARDY ADAM P; CLARIDGE TIMOTHY D W; HAMED REFAAT B; CHOWDHURY RASHEDUZZAMAN; GONG LINGZHI; ROBINSON CAROL V; TRUDGIAN DAVID C; JIANG MIAO; MACKEEN MUKRAM M; MCCULLAGH JAMES S; GORDIYENKO YULIYA; THALHAMMER ARMIN; YAMAMOTO ATSUSHI; YANG MING; LIUYI PHEBEE; ZHANG ZHIHONG; SCHMIDTZACHMANN MARION; KESSLER BENEDIKT M; RATCLIFFE PETER J; PRESTON GAIL M; COLEMAN MATHEW L; SCHOFIELD CHRISTOPHER J  
  选自 期刊  NATURE CHEMICAL BIOLOGY;  卷期  2012年8-12;  页码  960-962  
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[摘要]The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylation of the ribosomal protein Rpl16. Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively. This work reveals new therapeutic possibilities via oxygenase inhibition and by targeting modified over unmodified ribosomes.

 
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