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首页> 外文期刊>Journal of bacteriology >Structural Analysis of Mycobacterium tuberculosis Homologues of the Eukaryotic Proteasome Assembly Chaperone 2 (PAC2)
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Structural Analysis of Mycobacterium tuberculosis Homologues of the Eukaryotic Proteasome Assembly Chaperone 2 (PAC2)

机译：真核生物蛋白酶组装分子伴侣2（PAC2）的结核分枝杆菌同源物的结构分析。

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A previous bioinformatics analysis identified the Mycobacterium tuberculosis proteins Rv2125 and Rv2714 as orthologs of the eukaryotic proteasome assembly chaperone 2 (PAC2). We set out to investigate whether Rv2125 or Rv2714 can function in proteasome assembly. We solved the crystal structure of Rv2125 at a resolution of 3.0 ?, which showed an overall fold similar to that of the PAC2 family proteins that include the archaeal PbaB and the yeast Pba1. However, Rv2125 and Rv2714 formed trimers, whereas PbaB forms tetramers and Pba1 dimerizes with Pba2. We also found that purified Rv2125 and Rv2714 could not bind to M. tuberculosis 20S core particles. Finally, proteomic analysis showed that the levels of known proteasome components and substrate proteins were not affected by disruption of Rv2125 in M. tuberculosis. Our work suggests that Rv2125 does not participate in bacterial proteasome assembly or function.
机译：先前的生物信息学分析将结核分枝杆菌蛋白Rv2125和Rv2714鉴定为真核蛋白酶体装配伴侣2（PAC2）的直系同源物。我们着手研究Rv2125或Rv2714是否可以在蛋白酶体组装中起作用。我们以3.0？的分辨率解析了Rv2125的晶体结构，显示出与包括古细菌PbaB和酵母Pba1在内的PAC2家族蛋白相似的整体折叠。但是，Rv2125和Rv2714形成三聚体，而PbaB形成四聚体，而Pba1与Pba2二聚。我们还发现，纯化的Rv2125和Rv2714不能与结核分枝杆菌20S核心颗粒结合。最后，蛋白质组学分析表明，已知的蛋白酶体组分和底物蛋白的水平不受结核分枝杆菌中Rv2125的破坏影响。我们的工作表明Rv2125不参与细菌蛋白酶体的组装或功能。

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