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2001 | 48 | 2 | 337-350
Article title

Methionyl-tRNA synthetase.

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Abstracts
EN
Methionyl-tRNA synthetase (MetRS) belongs to the family of 20 enzymes essential for protein biosynthesis. It links covalently methionine with its cognate tRNA. Crystal structures solved for bacterial MetRSs have given a number of interesting insights into enzyme architecture and methionylation catalysis. A comparison of sequences of MetRSs belonging to all kingdoms of life, as well as numerous biochemical and genetic studies have revealed the presence of various additional domains appended to the catalytic core of synthetase. They are responsible for interactions with tRNA and proteins. Tertiary structure of C-terminal tRNA-binding appendices can be deduced from those determined for their homologues: tRNA binding protein 111 and endothelial monocyte-activating polypeptide II. Contacts between MetRS and other proteins could be mediated not only by noncatalytic peptides but also by structural elements present in the catalytic core, e.g. Arg-Gly-Asp (RGD) motifs. Additional activities involve MetRS in the maintenance of translational fidelity and in coordination of ribosome biogenesis with protein synthesis.
Publisher

Year
Volume
48
Issue
2
Pages
337-350
Physical description
Dates
published
2001
received
2001-02-14
accepted
2001-04-22
Contributors
  • Institute of Bioorganic Chemistry of the Polish Academy of Sciences, Poznań, Poland
  • Institute of Bioorganic Chemistry of the Polish Academy of Sciences, Poznań, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv48i2p337kz
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