Maf-dependent bacterial flagellin glycosylation occurs before chaperone binding and flagellar T3SS export.
Maf-dependent bacterial flagellin glycosylation occurs before chaperone binding and flagellar T3SS export.
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DOI:
10.1111/mmi.12549
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发表时间:
2014-04
影响因子:
3.6
通讯作者:
Shaw JG
中科院分区:
文献类型:
--
作者:
Parker JL;Lowry RC;Couto NA;Wright PC;Stafford GP;Shaw JG
Bacterial swimming is mediated by rotation of a filament that is assembled via polymerization of flagellin monomers after secretion via a dedicated flagellar Type III secretion system. Several bacteria decorate their flagellin with sialic acid related sugars that is essential for motility. Aeromonas caviae is a model organism for this process as it contains a genetically simple glycosylation system and decorates its flagellin with pseudaminic acid (Pse). The link between flagellin glycosylation and export has yet to be fully determined. We examined the role of glycosylation in the export and assembly process in a strain lacking Maf1, a protein involved in the transfer of Pse onto flagellin at the later stages of the glycosylation pathway. Immunoblotting, established that glycosylation is not required for flagellin export but is essential for filament assembly since non-glycosylated flagellin is still secreted. Maf1 interacts directly with its flagellin substrate in vivo, even in the absence of pseudaminic acid. Flagellin glycosylation in a flagellin chaperone mutant (flaJ) indicated that glycosylation occurs in the cytoplasm before chaperone binding and protein secretion. Preferential chaperone binding to glycosylated flagellin revealed its crucial role, indicating that this system has evolved to favour secretion of the polymerization competent glycosylated form.
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