論文 - 詳細
| RRC ID | 35640 |
|---|---|
| 著者 | Ge X, Wang R, Ma J, Liu Y, Ezemaduka AN, Chen PR, Fu X, Chang Z. |
| タイトル | DegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli. |
| ジャーナル | FEBS J |
| Abstract |
DegP (also designated as HtrA) and its homologs are found in prokaryotic cells and such eukaryotic organelles as mitochondria and chloroplasts. DegP has been found to be essential for the growth of Gram-negative bacteria under heat shock conditions and arguably considered to possess both protease and chaperone activities. The function of DegP has not been clearly defined. Using genetically incorporated non-natural amino acids as photo-crosslinkers, here we identified the β-barrel outer membrane proteins (OMPs) as the major natural substrates of DegP in Escherichia coli cells. We also demonstrated that DegP primarily functions as a protease, at both low and high temperatures, to eliminate unfolded OMPs, with hardly any appreciable chaperone activity in cells. We also found that the toxic and cell membrane-damaging misfolded OMPs would accumulate in DegP-lacking cells cultured under heat shock conditions. Together, our study defines the primary function of DegP in OMP biogenesis and offers a mechanistic insight into the essentiality of DegP for cell growth under heat shock conditions. |
| 巻・号 | 281(4) |
| ページ | 1226-40 |
| 公開日 | 2014-2-1 |
| DOI | 10.1111/febs.12701 |
| PMID | 24373465 |
| MeSH | Bacterial Outer Membrane Proteins / metabolism* Escherichia coli / metabolism* Escherichia coli Proteins / metabolism* Heat-Shock Proteins / metabolism* Periplasmic Proteins / metabolism* Serine Endopeptidases / metabolism* |
| IF | 4.392 |
| 引用数 | 40 |
| WOS 分野 | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| 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 | 1 |
| 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) | ME9062(BW25113) JW0157-KC JW0052-KC |