| Literature DB >> 27745969 |
Fange Liu1, Wesley Clark2, Guanzheng Luo1, Xiaoyun Wang2, Ye Fu1, Jiangbo Wei1, Xiao Wang1, Ziyang Hao1, Qing Dai1, Guanqun Zheng2, Honghui Ma1, Dali Han1, Molly Evans2, Arne Klungland3, Tao Pan4, Chuan He5.
Abstract
tRNA is a central component of protein synthesis and the cell signaling network. One salient feature of tRNA is its heavily modified status, which can critically impact its function. Here, we show that mammalian ALKBH1 is a tRNA demethylase. It mediates the demethylation of N1-methyladenosine (m1A) in tRNAs. The ALKBH1-catalyzed demethylation of the target tRNAs results in attenuated translation initiation and decreased usage of tRNAs in protein synthesis. This process is dynamic and responds to glucose availability to affect translation. Our results uncover reversible methylation of tRNA as a new mechanism of post-transcriptional gene expression regulation.Entities:
Keywords: ALKBH1; N(1)-methyladenosine (m(1)A); codon usage; dynamic tRNA modification; tRNA demethylase; tRNA demethylation; tRNA methylation; translation elongation; translation initiation; translation regulation
Mesh:
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Year: 2016 PMID: 27745969 PMCID: PMC5119773 DOI: 10.1016/j.cell.2016.09.038
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582