Karlinsey J E, Lonner J, Brown K L, Hughes K T
Department of Microbiology, University of Washington, Seattle 98195, USA.
Cell. 2000 Aug 18;102(4):487-97. doi: 10.1016/s0092-8674(00)00053-2.
Type III secretion systems mediate export of virulence proteins and flagellar assembly subunits in Gram-negative bacteria. Chaperones specific to each class of secreted protein are believed to prevent degradation of the secreted substrates. We show that an additional role of chaperones may be to regulate translation of secreted proteins. We show that the chaperone FIgN is required for translation of the flgM gene transcribed from one mRNA transcript (a flagellar class 3 transcript), but not from another (a flagellar class 2 transcript). FIgM translated from the class 3 transcript is primarily secreted whereas FIgM translated from the class 2 transcript is primarily retained in the cytoplasm. These results suggest FIgM and other type III secretion substrates possess both mRNA and amino acid secretion signals, and supports a new role for type III chaperones in translation/secretion coupling.
III型分泌系统介导革兰氏阴性菌中毒力蛋白和鞭毛组装亚基的输出。据信,每种分泌蛋白类别的特异性伴侣蛋白可防止分泌底物的降解。我们发现,伴侣蛋白的另一个作用可能是调节分泌蛋白的翻译。我们发现,伴侣蛋白FIgN是从一个mRNA转录本(鞭毛3类转录本)转录的flgM基因翻译所必需的,但从另一个转录本(鞭毛2类转录本)转录的flgM基因翻译则不需要。从3类转录本翻译的FIgM主要被分泌,而从2类转录本翻译的FIgM主要保留在细胞质中。这些结果表明,FIgM和其他III型分泌底物同时具有mRNA和氨基酸分泌信号,并支持III型伴侣蛋白在翻译/分泌偶联中的新作用。