Shotgun EM of mycobacterial protein complexes during stationary phase stress.
Shotgun EM of mycobacterial protein complexes during stationary phase stress.
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DOI：
10.1016/j.crstbi.2020.09.002
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发表时间：
2020
影响因子：
2.8
通讯作者：
Woodward JD
中科院分区：
文献类型：
--
作者：
Kirykowicz AM;Woodward JD
There is little structural information about the protein complexes conferring resistance in Mycobacterium tuberculosis (Mtb) to anti-microbial oxygen and nitrogen radicals in the phagolysosome. Here, we expose the model Mycobacterium, Mycobacterium smegmatis, to simulated oxidative-stress conditions and apply a shotgun EM method for the structural detection of the resulting protein assemblies. We identified: glutamine synthetase I, essential for Mtb virulence; bacterioferritin A, critical for Mtb iron regulation; aspartyl aminopeptidase M18, a protease; and encapsulin, which produces a cage-like structure to enclose cargo proteins. After further investigation, we found that encapsulin carries dye-decolourising peroxidase, a protein antioxidant, as its primary cargo under the conditions tested. Induce oxidative stress response in Mycobacterium smegmatis. Applied shotgun electron microscopy to find native protein complexes. Relion single particle reconstruction and identify by mass spectrometry. Found four protein complexes: encapsulin, GSI, BfrA, apeB. Encapsulin encloses dye-decolourising type peroxidase, an enzymatic antioxidant.
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