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Regulation of chaperone/effector complex synthesis in a bacterial type III secretion system
Author(s) -
Button Julie E.,
Galán Jorge E.
Publication year - 2011
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2011.07784.x
Subject(s) - chaperone (clinical) , effector , biology , secretion , microbiology and biotechnology , type three secretion system , translation (biology) , salmonella , bacteria , genetics , computational biology , biochemistry , messenger rna , gene , virulence , medicine , pathology
Summary Type III protein secretion systems (T3SSs), which have evolved to deliver bacterial proteins into nucleated cells, are found in many species of Gram‐negative bacteria that live in close association with eukaryotic hosts. Proteins destined to travel this secretion pathway are targeted to the secretion machine by customized chaperones, with which they form highly structured complexes. Here, we have identified a mechanism that co‐ordinates the expression of the Salmonella Typhimurium T3SS chaperone SicP and its cognate effector SptP. Translation of the effector is coupled to that of its chaperone, and in the absence of translational coupling, an inhibitory RNA structure prevents translation of sptP . The data presented here show how the genomic organization of functionally related proteins can have a significant impact on the co‐ordination of their expression.