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Activation of the pyrrolysine suppressor tRNA requires formation of a ternary complex with class I and class II lysyl-tRNA synthetases.
- Source :
-
Molecular cell [Mol Cell] 2003 Aug; Vol. 12 (2), pp. 287-94. - Publication Year :
- 2003
-
Abstract
- Monomethylamine methyltransferase of the archaeon Methanosarcina barkeri contains a rare amino acid, pyrrolysine, encoded by the termination codon UAG. Translation of this UAG requires the aminoacylation of the corresponding amber suppressor tRNAPyl. Previous studies reported that tRNAPyl could be aminoacylated by the synthetase-like protein PylS. We now show that tRNAPyl is efficiently aminoacylated in the presence of both the class I LysRS and class II LysRS of M. barkeri, but not by either enzyme acting alone or by PylS. In vitro studies show that both the class I and II LysRS enzymes must bind tRNAPyl in order for the aminoacylation reaction to proceed. Structural modeling and selective inhibition experiments indicate that the class I and II LysRSs form a ternary complex with tRNAPyl, with the aminoacylation activity residing in the class II enzyme.
- Subjects :
- Archaeal Proteins
Base Sequence
Codon, Terminator
DNA metabolism
Lysine metabolism
Methanosarcina barkeri enzymology
Methyltransferases chemistry
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Biosynthesis
RNA, Transfer metabolism
Time Factors
Transcription, Genetic
Lysine analogs & derivatives
Lysine chemistry
Lysine-tRNA Ligase chemistry
RNA, Transfer chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1097-2765
- Volume :
- 12
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 14536069
- Full Text :
- https://doi.org/10.1016/s1097-2765(03)00280-6