論文 - 詳細
| RRC ID | 53723 |
|---|---|
| 著者 | Yanagisawa T, Takahashi H, Suzuki T, Masuda A, Dohmae N, Yokoyama S. |
| タイトル | Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability. |
| ジャーナル | PLoS One |
| Abstract |
Translation elongation factor P (EF-P), a ubiquitous protein over the entire range of bacterial species, rescues ribosomal stalling at consecutive prolines in proteins. In Escherichia coli and Salmonella enterica, the post-translational β-lysyl modification of Lys34 of EF-P is important for the EF-P activity. The β-lysyl EF-P modification pathway is conserved among only 26-28% of bacteria. Recently, it was found that the Shewanella oneidensis and Pseudomonas aeruginosa EF-P proteins, containing an Arg residue at position 32, are modified with rhamnose, which is a novel post-translational modification. In these bacteria, EF-P and its Arg modification are both dispensable for cell viability, similar to the E. coli and S. enterica EF-P proteins and their Lys34 modification. However, in the present study, we found that EF-P and Arg32 are essential for the viability of the human pathogen, Neisseria meningitidis. We therefore analyzed the modification of Arg32 in the N. meningitidis EF-P protein, and identified the same rhamnosyl modification as in the S. oneidensis and P. aeruginosa EF-P proteins. N. meningitidis also has the orthologue of the rhamnosyl modification enzyme (EarP) from S. oneidensis and P. aeruginosa. Therefore, EarP should be a promising target for antibacterial drug development specifically against N. meningitidis. The pair of genes encoding N. meningitidis EF-P and EarP suppressed the slow-growth phenotype of the EF-P-deficient mutant of E. coli, indicating that the activity of N. meningitidis rhamnosyl-EF-P for rescuing the stalled ribosomes at proline stretches is similar to that of E. coli β-lysyl-EF-P. The possible reasons for the unique requirement of rhamnosyl-EF-P for N. meningitidis cells are that more proline stretch-containing proteins are essential and/or the basal ribosomal activity to synthesize proline stretch-containing proteins in the absence of EF-P is lower in this bacterium than in others. |
| 巻・号 | 11(2) |
| ページ | e0147907 |
| 公開日 | 2016-1-1 |
| DOI | 10.1371/journal.pone.0147907 |
| PII | PONE-D-15-25534 |
| PMID | 26840407 |
| PMC | PMC4739656 |
| MeSH | Amino Acid Sequence Anti-Bacterial Agents / pharmacology Arginine / chemistry Arginine / metabolism* Biological Evolution Catalytic Domain / genetics* Gene Deletion Genome, Bacterial Glycosylation Humans Microbial Viability / genetics* Molecular Sequence Data Neisseria meningitidis / drug effects Neisseria meningitidis / physiology* Peptide Elongation Factors / chemistry Peptide Elongation Factors / genetics* Peptide Elongation Factors / metabolism* Proline / metabolism Protein Processing, Post-Translational / drug effects Rhamnose / metabolism Ribosomes / metabolism Tandem Mass Spectrometry |
| IF | 2.74 |
| 引用数 | 22 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 2 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 原核生物(大腸菌) | |