DegP degrades a wide range of substrate proteins in Escherichia coli under stress conditions.
DegP degrades a wide range of substrate proteins in Escherichia coli under stress conditions.
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在应激条件下，DegP 可降解大肠杆菌中的多种底物蛋白。
DOI：
10.1042/bcj20190446
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发表时间：
2019-11
影响因子：
4.1
通讯作者：
Fu Xinmiao
中科院分区：
文献类型：
--
作者：
Zhang Shuang;Cheng Yu;Ma Jing;Wang Yan;Chang Zengyi;Fu Xinmiao
DegP是革兰氏阴性菌中的一种周质双功能蛋白酶和分子伴侣，对细菌的抗逆性至关重要，但其确切的潜在机制尚未完全了解。在这里，我们表明DegP的蛋白酶功能对于大肠杆菌细胞保持膜完整性是至关重要的，特别是在热休克条件下（42 ° C）。定点光交联、质谱和免疫印迹分析显示，两种周质蛋白（例如，OppA和MalE）和β-桶外膜蛋白（OMP）是DegP相互作用蛋白，并且OppA在体外和体内在42 ℃下被DegP降解。此外，OmpA和BamA（含有可溶性周质结构域的嵌合β-桶OMP）以未折叠和折叠形式与DegP结合，而只有未折叠形式可被DegP降解。作为DegP底物的折叠OmpA的存在归因于其周质结构域，其对DegP降解具有抗性，甚至通常以分子内方式保护纯β-桶OMP免于降解。此外，DegP的PDZ结构域-1中的一对残基（R262和V328）对于结合未折叠和折叠的β-桶OMP起重要作用，其中R262是关键的。我们的研究与早期的报道一起表明，DegP通过在应激条件下降解周质蛋白和β-桶OMP，并且可能还通过参与嵌合β-桶OMP的折叠，在细菌周质中的蛋白质质量控制中起关键作用。提出了一个工作模型来说明DegP相对于不同底物蛋白的微调功能。
DegP, a periplasmic dual-functional protease and chaperone in Gram-negative bacteria, is critical for bacterial stress resistance, but the precise underlying mechanisms are not fully understood. Here, we show that the protease function of DegP is critical for Escherichia coli cells to maintain membrane integrity, particularly under heat shock conditions (42{degree sign}C). Site-directed photo-crosslinking, mass spectrometry, and immunoblotting analyses reveal that both periplasmic proteins (e.g., OppA and MalE) and β-barrel outer membrane proteins (OMPs) are DegP-interacting proteins and that OppA is degraded by DegP in vitro and in vivo at 42{degree sign}C. In addition, OmpA and BamA, chimeric β-barrel OMPs containing a soluble periplasmic domain, are bound to DegP in both unfolded and folded forms, whereas only the unfolded forms are degradable by DegP. The presence of folded OmpA as a substrate of DegP is attributed to its periplasmic domain, which is resistant to DegP degradation and even generally protects pure β-barrel OMPs from degradation in an intra-molecular way. Further, a pair of residues (R262 and V328) in the PDZ domain-1 of DegP play important roles for binding unfolded and folded β-barrel OMPs, with R262 being critical. Our study, together with earlier reports, indicates that DegP plays a critical role in protein quality control in the bacterial periplasm by degrading both periplasmic proteins and β-barrel OMPs under stress conditions and likely also by participating in the folding of chimeric β-barrel OMPs. A working model is proposed to illustrate the finely tuned functions of DegP with respect to different substrate proteins.
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影响因子：
3.1
作者：
Jones, CH;Bolken, TC;Hruby, DE
通讯作者：
Hruby, DE
DOI：
10.1007/978-94-011-2108-8
发表时间：
1996-02
期刊：
--
影响因子：
--
作者：
R. A. Laskey
通讯作者：
R. A. Laskey
DOI：
10.1016/s0021-9258(18)92740-7
发表时间：
1991-07
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
R. Misra;A. Peterson;T. Ferenci;T. Silhavy
通讯作者：
R. Misra;A. Peterson;T. Ferenci;T. Silhavy
影响因子：
3.2
作者：
Gao, Tao;O'Brian, Mark R.
通讯作者：
O'Brian, Mark R.
DOI：
10.1007/s004380051092
发表时间：
1999-09
期刊：
Molecular and General Genetics MGG
影响因子：
--
作者：
J. Skórko-Glonek;D. Zurawa;E. Kuczwara;M. Wozniak;Z. Wypych;B. Lipińska
通讯作者：
J. Skórko-Glonek;D. Zurawa;E. Kuczwara;M. Wozniak;Z. Wypych;B. Lipińska