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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Lon and Clp family proteases and chaperones share homologous substrate-recognition domains
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Lon and Clp family proteases and chaperones share homologous substrate-recognition domains

机译：Lon和Clp家族的蛋白酶和分子伴侣共享同源的底物识别域

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摘要

Lon protease and members of the Clp family or molecular chaperones and protease regulatory subunits contain homologous regions with properties expected for substrate-binding domains. Fragments corresponding to these sequences are stably and independently folded for Lon, ClpA,and ClpY. The corresponding regions from ClpB and ClpX are unstable. All five fragments exbibit distinct patterns of binding to three proteins that are protease substrates in vivo: the heat shock transcription factor #sigma#~(32), the SOS mu- tagenesis protein UmuD, and Arc repressor bearing the SsrA degradation tag. Recognition of UmuD is mediated through peptide sequences within a 24-residue N-terminal region whereas recognition of both #sigma#~(32) and SsrA-tagged Arc requires sequences at the C terminus. These results indicate that the Lon and Clp proteases use the same mechanism of substrate discrimination and suggest that these related ATP-dependent bacterial proteases scrutinize accessible or disordered regions of potential substrates for the presence of specific targeting sequences.
机译：Lon蛋白酶和Clp家族成员或分子伴侣和蛋白酶调节亚基包含同源区域，具有预期的底物结合域特性。对应于这些序列的片段被稳定且独立地折叠成Lon，ClpA和ClpY。 ClpB和ClpX的相应区域不稳定。所有这五个片段都在体内与三种蛋白质（蛋白酶底物）结合的结合模式不同：热休克转录因子＃sigma＃〜（32），SOS诱变蛋白UmuD和带有SsrA降解标签的Arc阻遏物。 UmuD的识别是通过24个残基N端区域内的肽序列介导的，而＃sigma＃〜（32）和SsrA标记的Arc的识别都需要C端的序列。这些结果表明，Lon和Clp蛋白酶使用相同的底物识别机制，并表明这些相关的ATP依赖性细菌蛋白酶会仔细检查潜在底物的可及区域或无序区域是否存在特定的靶向序列。

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