Involvement of the GspAB complex in assembly of the type II secretion system secretin of Aeromonas and Vibrio species.
Involvement of the GspAB complex in assembly of the type II secretion system secretin of Aeromonas and Vibrio species.
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GspAB 复合物参与气单胞菌和弧菌 II 型分泌系统促胰液素的组装。
DOI：
10.1128/jb.01413-10
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发表时间：
2011
影响因子：
3.2
通讯作者：
Howard,SPeter
中科院分区：
文献类型：
--
作者：
Strozen,TimothyG;Stanley,Heather;Gu,Yuqi;Boyd,Jessica;Bagdasarian,Michael;Sandkvist,Maria;Howard,SPeter
The type II secretion system (T2SS) functions as a transport mechanism to translocate proteins from the periplasm to the extracellular environment. The ExeA homologue in Aeromonas hydrophila, GspAAh, is an ATPase that interacts with peptidoglycan and forms an inner membrane complex with the ExeB homologue (GspBAh). The complex may be required to generate space in the peptidoglycan mesh that is necessary for the transport and assembly of the megadalton-sized ExeD homologue (GspDAh) secretin multimer in the outer membrane. In this study, the requirement for GspAB in the assembly of the T2SS secretin in Aeromonas and Vibrio species was investigated. We have demonstrated a requirement for GspAB in T2SS assembly in Aeromonas salmonicida, similar to that previously observed in A. hydrophila. In the Vibrionaceae species Vibrio cholerae, Vibrio vulnificus, and Vibrio parahaemolyticus,gspAmutations significantly decreased assembly of the secretin multimer but had minimal effects on the secretion of T2SS substrates. The lack of effect on secretion of the mutant ofgspAof V. cholerae (gspAVc) was explained by the finding that native secretin expression greatly exceeds the level needed for efficient secretion in V. cholerae. In cross-complementation experiments, secretin assembly and secretion in anA. hydrophila gspAmutant were partially restored by the expression of GspAB from V. cholerae intrans, further suggesting that GspABVcperforms the same role in Vibrio species as GspABAhdoes in the aeromonads. These results indicate that the GspAB complex is functional in the assembly of the secretin in Vibrio species but that a redundancy of GspAB function may exist in this genus.
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