Translation elongation factor EF-Tu modulates filament formation of actin-like MreB protein in vitro.
Translation elongation factor EF-Tu modulates filament formation of actin-like MreB protein in vitro.
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翻译延伸因子 EF-Tu 体外调节肌动蛋白样 MreB 蛋白丝的形成
DOI：
10.1016/j.jmb.2015.01.025
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发表时间：
2015
影响因子：
5.6
通讯作者：
Graumann PL
中科院分区：
文献类型：
--
作者：
Defeu Soufo HJ;Reimold C;Breddermann H;Mannherz HG;Graumann PL
EF-Tu has been shown to interact with actin-like protein MreB and to affect its localization inEscherichia coliand inBacillus subtiliscells. We have purified YFP-MreB in an active form, which forms filaments on glass slidesin vitroand was active in dynamic light-scattering assays, polymerizing in milliseconds after addition of magnesium. Purified EF-Tu enhanced the amount of MreB filaments, as seen by sedimentation assays, the speed of filament formation and the length of MreB filamentsin vitro. EF-Tu had the strongest impact on MreB filaments in a 1:1 ratio, and EF-Tu co-sedimented with MreB filaments, revealing a stoichiometric interaction between both proteins. This was supported by cross-linking assays where 1:1 species were well detectable. When expressed inE.colicells,B.subtilisMreB formed filaments and induced the formation of co-localizingB.subtilisEF-Tu structures, indicating that MreB can direct the positioning of EF-Tu structures in a heterologous cell system. Fluorescence recovery after photobleaching analysis showed that MreB filaments have a higher turnover inB.subtiliscells than inE.colicells, indicating different filament kinetics in homologous or heterologous cell systems. The data show that MreB can direct the localization of EF-Tuin vivo, which in turn positively affects the formation and dynamics of MreB filaments. Thus, EF-Tu is a modulator of the activity of a bacterial actin-like protein.
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DOI：
10.1073/pnas.0507708102
发表时间：
2005-12-20
影响因子：
11.1
作者：
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通讯作者：
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影响因子：
2.1
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通讯作者：
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影响因子：
2.1
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通讯作者：
Ishihama, A
影响因子：
7.7
作者：
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通讯作者：
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