Chloroplast Omp85 proteins change orientation during evolution
Chloroplast Omp85 proteins change orientation during evolution
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叶绿体 Omp85 蛋白在进化过程中改变方向
DOI:
10.1073/pnas.1108626108
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发表时间:
2011
期刊:
影响因子:
--
通讯作者:
Schleiff E
中科院分区:
文献类型:
--
作者:
Sommer MS;Daum B;Gross LE;Weis BLM;Mirus O;Abram L;Maier UG;Kühlbrandt W;Schleiff E
The majority of outer membrane proteins (OMPs) from Gram-negative bacteria and many of mitochondria and chloroplasts are β-barrels. Insertion and assembly of these proteins are catalyzed by the Omp85 protein family in a seemingly conserved process. All members of this family exhibit a characteristic N-terminal polypeptide-transport–associated (POTRA) and a C-terminal 16-stranded β-barrel domain. In plants, two phylogenetically distinct and essential Omp85's exist in the chloroplast outer membrane, namely Toc75-III and Toc75-V. Whereas Toc75-V, similar to the mitochondrial Sam50, is thought to possess the original bacterial function, its homolog, Toc75-III, evolved to the pore-forming unit of the TOC translocon for preprotein import. In all current models of OMP biogenesis and preprotein translocation, a topology of Omp85 with the POTRA domain in the periplasm or intermembrane space is assumed. Using self-assembly GFP-based in vivo experiments and in situ topology studies by electron cryotomography, we show that the POTRA domains of both Toc75-III and Toc75-V are exposed to the cytoplasm. This unexpected finding explains many experimental observations and requires a reevaluation of current models of OMP biogenesis and TOC complex function.
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DOI:
10.1016/j.str.2010.08.012
发表时间:
2010-11-10
期刊:
Structure (London, England : 1993)
影响因子:
--
作者:
Gatzeva-Topalova PZ;Warner LR;Pardi A;Sousa MC
通讯作者:
Sousa MC
DOI:
10.1073/pnas.92.16.7177
发表时间:
1995
影响因子:
11.1
作者:
VanderVere,PS;Bennett,TM;Oblong,JE;Lamppa,GK
通讯作者:
Lamppa,GK
影响因子:
5.3
作者:
Carrie C;Murcha MW;Whelan J
通讯作者:
Whelan J
影响因子:
3
作者:
Frangakis, AS;Hegerl, R
通讯作者:
Hegerl, R
影响因子:
27.5
作者:
N. Sveshnikova;Rudolf Grimm;Jürgen Soll;Enrico Schleiff
通讯作者:
Enrico Schleiff