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PMID: 10966110 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Translation/secretion coupling by type III secretion systems.

Cell ·Vol. 102 ·No. 4 ·2000-08-18 ·Pages 487-97

Karlinsey JE, Lonner J, Brown KL, Hughes KT

Abstract

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.

MeSH Terms
Bacterial Proteins/genetics,physiology Gene Expression Regulation, Bacterial Gram-Negative Bacteria/genetics,pathogenicity Molecular Chaperones/physiology Promoter Regions, Genetic Protein Biosynthesis Transcription, Genetic
Chemicals
Bacterial Proteins FlgN protein, Bacteria Molecular Chaperones FlgM protein, Bacteria
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Karlinsey J E
Department of Microbiology, University of Washington, Seattle 98195, USA.
Lonner J
Brown K L
Hughes K T
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
2000-08-18
Pages
487-97
Language
English
Region
United States
NLM ID
0413066
Subset
IM
Grants
NIGMS NIH HHS · GM43149 · United States
NIGMS NIH HHS · GM56141 · United States
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