| RRC ID |
35295
|
| 著者 |
Yanagisawa T, Sumida T, Ishii R, Takemoto C, Yokoyama S.
|
| タイトル |
A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P.
|
| ジャーナル |
Nat Struct Mol Biol
|
| Abstract |
Aminoacyl-tRNA synthetase (aaRS) paralogs with unknown functions exist in various species. We now report novel 'protein lysylation' by an Escherichia coli lysyl-tRNA synthetase paralog, GenX/PoxA/YjeA. X-ray crystallographic analysis shows that the structure of the GenX protein resembles that of a class II aaRS. Further in vitro studies reveal that it specifically aminoacylates EF-P with lysine. The shape of the protein substrate mimics that of the L-shaped tRNA, and its lysylation site corresponds to the tRNA 3' end. Thus, we show how the aaRS architecture can be adapted to achieve aminoacylation of a specific protein. Moreover, in vivo analyses reveal that the translation elongation factor P (EF-P) lysylation by GenX is enhanced by YjeK (lysine 2,3-aminomutase paralog), which is encoded next to the EF-P gene, and might convert alpha-lysyl-EF-P to beta-lysyl-EF-P. In vivo analyses indicate that the EF-P modification by GenX and YjeK is essential for cell survival.
|
| 巻・号 |
17(9)
|
| ページ |
1136-43
|
| 公開日 |
2010-9-1
|
| DOI |
10.1038/nsmb.1889
|
| PII |
nsmb.1889
|
| PMID |
20729861
|
| MeSH |
Aminoacylation
Animals
Crystallography, X-Ray
Escherichia coli / enzymology*
Humans
Lysine / metabolism
Lysine-tRNA Ligase / chemistry*
Lysine-tRNA Ligase / genetics
Lysine-tRNA Ligase / metabolism
Models, Molecular
Mutation
Peptide Elongation Factors / chemistry*
Peptide Elongation Factors / genetics
Peptide Elongation Factors / metabolism
Phylogeny
Protein Binding
Protein Processing, Post-Translational
Protein Structure, Quaternary
Protein Structure, Tertiary
|
| IF |
11.98
|
| 引用数 |
93
|
|
WOS 分野
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
CELL BIOLOGY
|
| リソース情報 |
| 原核生物(大腸菌) |
JW4107-KC
JW4116-KC |
