FlgM proteins from different bacteria exhibit different structural characteristics.
FlgM proteins from different bacteria exhibit different structural characteristics.
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DOI：
10.1016/j.bbapap.2013.01.010
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发表时间：
2013-04
影响因子：
3.2
通讯作者：
Gage, Matthew J.
中科院分区：
文献类型：
--
作者：
Ma, Wai Kit;Hendrix, Rachel;Stewart, Claire;Campbell, Eric V.;Lavarias, Mitchell;Morris, Kolyn;Nichol, Shauna;Gage, Matthew J.
本质性无序蛋白质（IDP）是一类独特的蛋白质，其功能不需要稳定的结构。IDP在许多生物过程中的重要性已经被确立，但关于它们在蛋白质家族中的进化和无序状态的保持仍有未解答的问题。我们的研究小组一直在研究直向同源FlgM蛋白（IDP的一个模型类别）之间的结构相似性。我们先前已经表明，来自嗜热菌风产液菌的FlgM蛋白在A处具有更多的结构。aeolicus的生理温度（85 °C）高于鼠伤寒沙门氏菌FlgM，表明FlgM的无序性质在生物体中不同，并不是普遍保守的。在这项工作中，我们将这些研究扩展到大肠杆菌、铜绿假单胞菌、奇异变形杆菌和枯草芽孢杆菌的FlgM蛋白。我们证明了B.枯草芽孢杆菌E. subtilis coli和S.鼠伤寒沙门氏菌FlgMs以预熔融的球状构象存在，而B.枯草芽孢杆菌FlgM的构象比其它两种更紧凑。铜绿假单胞菌和奇异假单胞菌FlgM蛋白质以目前未知的构象存在，该构象既不是螺旋样也不是预熔融小球样。铜绿假单胞菌FlgM看起来含有更弱的分子内接触，因为其比奇异假单胞菌FlgM具有更紧密的状态。这些结果提供了实验证据，证明同一蛋白质家族的成员可以表现出不同程度的无序，尽管要了解同一蛋白质家族中不同无序状态是如何演变的还需要更多的研究。
Intrinsically disordered proteins (IDPs) are a unique class of proteins that do not require a stable structure for function. The importance of IDPs in many biological processes has been established but there remain unanswered questions about their evolution and conservation of their disordered state within a protein family. Our group has been studying the structural similarities among orthologous FlgM proteins, a model class of IDPs. We have previously shown that the FlgM protein from the thermophile Aquifex aeolicus has more structure at A. aeolicus' physiological temperature (85 °C) than is observed for the Salmonella typhimurium FlgM, suggesting that the disordered nature of FlgM varies among organisms and is not universally conserved. In this work, we extend these studies to the FlgM proteins from Escherichia coli, Pseudomonas aeruginosa, Proteus mirabilis, and Bacillus subtilis. We demonstrate that the B. subtilis, E. coli, and S. typhimurium FlgMs exist in a premolten globule-like conformation, though the B. subtilis FlgM is in a more compacted conformation than the other two. The P. aeruginosa and P. mirabilis FlgM proteins exist in a currently unknown conformation that is not either coil-like or premolten globule-like. The P. aeruginosa FlgM appears to contain more weak intramolecular contacts given its more compacted state than the P. mirabilis FlgM. These results provide experimental evidence that members of the same protein family can exhibit different degrees of disorder, though understanding how different disordered states evolve in the same protein family will require more study.
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DOI：
10.1016/s0006-291x(71)80225-5
发表时间：
1971-01-01
影响因子：
3.1
作者：
CHEN, YH;YANG, JT
通讯作者：
YANG, JT
影响因子：
2.9
作者：
Dunker, AK;Lawson, JD;Obradovic, Z
通讯作者：
Obradovic, Z
影响因子：
5.6
作者：
Campbell, EA;Darst, SA
通讯作者：
Darst, SA
影响因子：
3.2
作者：
Correa, NE;Barker, JR;Klose, KE
通讯作者：
Klose, KE
DOI：
10.1023/a:1026397008011
发表时间：
1997-07-01
期刊：
JOURNAL OF PROTEIN CHEMISTRY
影响因子：
--
作者：
Chaffotte, AF;Guijarro, JI;Goldberg, ME
通讯作者：
Goldberg, ME