The domain organization of the bacterial intermediate filament-like protein crescentin is important for assembly and function.
The domain organization of the bacterial intermediate filament-like protein crescentin is important for assembly and function.
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DOI：
10.1002/cm.20505
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发表时间：
2011-04
期刊：
影响因子：
2.9
通讯作者：
Jacobs-Wagner, Christine
中科院分区：
文献类型：
--
作者：
Cabeen, Matthew T.;Herrmann, Harald;Jacobs-Wagner, Christine
Crescentin是一种细菌毒素形成蛋白，其表现出在后生动物中间丝（IF）蛋白中发现的结构域组织特征。由于缺乏简单的遗传系统和易于定量的表型，真核生物干扰素的结构-功能研究受到阻碍。在这里，我们利用的新月结构沿着新月柄杆菌细胞的内曲率和细胞曲率的损失与受损的新月功能的新月域组织的重要性进行分析的特征本地化。通过结合生物化学和超微结构分析，在体外细胞定位和功能研究，我们表明，新月需要其独特的结构域组织，而且，不同的结构元素有不同的结构和功能的贡献。头部结构域可以在功能上细分为两个亚结构域;第一个（氨基末端）是功能所需的，但不是组装所需的，而第二个是结构组装所需的。杆状结构域同样需要结构组装，并且接头L1对于防止失控组装成非功能性聚集体似乎很重要。这些数据还表明，口吃和尾部结构域具有关键的功能作用，在稳定的新月体结构，防止拆卸的一价阳离子在细胞质中。这项研究表明，IF样行为的新月形是其结构域组织的结果，这意味着IF蛋白布局是一个适应性细胞骨架基序，很像肌动蛋白和微管蛋白折叠，广泛利用从细菌到人类的各种功能。© 2011 Wiley-Liss公司。
Crescentin is a bacterial filament-forming protein that exhibits domain organization features found in metazoan intermediate filament (IF) proteins. Structure-function studies of eukaryotic IFs have been hindered by a lack of simple genetic systems and easily quantifiable phenotypes. Here we exploit the characteristic localization of the crescentin structure along the inner curvature of Caulobacter crescentus cells and the loss of cell curvature associated with impaired crescentin function to analyze the importance of the domain organization of crescentin. By combining biochemistry and ultrastructural analysis in vitro with cellular localization and functional studies, we show that crescentin requires its distinctive domain organization, and furthermore that different structural elements have distinct structural and functional contributions. The head domain can be functionally subdivided into two subdomains; the first (amino-terminal) is required for function but not assembly, while the second is necessary for structure assembly. The rod domain is similarly required for structure assembly, and the linker L1 appears important to prevent runaway assembly into nonfunctional aggregates. The data also suggest that the stutter and the tail domain have critical functional roles in stabilizing crescentin structures against disassembly by monovalent cations in the cytoplasm. This study suggests that the IF-like behavior of crescentin is a consequence of its domain organization, implying that the IF protein layout is an adaptable cytoskeletal motif, much like the actin and tubulin folds, that is broadly exploited for various functions throughout life from bacteria to humans. © 2011 Wiley-Liss, Inc.
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影响因子：
64.8
作者：
DEBOER, P;CROSSLEY, R;ROTHFIELD, L
通讯作者：
ROTHFIELD, L
影响因子：
10.5
作者：
Charbon, Godefroid;Cabeen, Matthew T.;Jacobs-Wagner, Christine
通讯作者：
Jacobs-Wagner, Christine
影响因子：
5.8
作者：
Delorenzi, M;Speed, T
通讯作者：
Speed, T
影响因子：
5.6
作者：
Baer, Harald;Schopferer, Michael;Willenbacher, Norbert
通讯作者：
Willenbacher, Norbert
DOI：
10.1073/pnas.0402638101
发表时间：
2004-06-08
影响因子：
11.1
作者：
Gitai, Z;Dye, N;Shapiro, L
通讯作者：
Shapiro, L