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S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates.
Han, Lu; Marcus, Erin; D'Silva, Sonia; Phizicky, Eric M.
Affiliation
  • Han L; Department of Biochemistry and Biophysics, Center for RNA Biology, University of Rochester School of Medicine, Rochester, New York 14642, USA.
  • Marcus E; Department of Biochemistry and Biophysics, Center for RNA Biology, University of Rochester School of Medicine, Rochester, New York 14642, USA.
  • D'Silva S; Department of Biochemistry and Biophysics, Center for RNA Biology, University of Rochester School of Medicine, Rochester, New York 14642, USA.
  • Phizicky EM; Department of Biochemistry and Biophysics, Center for RNA Biology, University of Rochester School of Medicine, Rochester, New York 14642, USA.
RNA ; 23(3): 406-419, 2017 03.
Article in En | MEDLINE | ID: mdl-28003514
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: TRNA Methyltransferases / Saccharomyces cerevisiae / Anticodon / RNA, Transfer, Ser / Cytidine / Saccharomyces cerevisiae Proteins / Microfilament Proteins Language: En Journal: RNA Journal subject: BIOLOGIA MOLECULAR Year: 2017 Document type: Article Affiliation country: Country of publication:
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: TRNA Methyltransferases / Saccharomyces cerevisiae / Anticodon / RNA, Transfer, Ser / Cytidine / Saccharomyces cerevisiae Proteins / Microfilament Proteins Language: En Journal: RNA Journal subject: BIOLOGIA MOLECULAR Year: 2017 Document type: Article Affiliation country: Country of publication: