PMID- 17526852
OWN - NLM
STAT- MEDLINE
DCOM- 20071105
LR  - 20200826
IS  - 1350-0872 (Print)
IS  - 1350-0872 (Linking)
VI  - 153
IP  - Pt 6
DP  - 2007 Jun
TI  - EscC is a chaperone for the Edwardsiella tarda type III secretion system putative 
      translocon components EseB and EseD.
PG  - 1953-1962
LID - 10.1099/mic.0.2006/004952-0 [doi]
AB  - Edwardsiella tarda is a Gram-negative enteric pathogen that causes disease in 
      both humans and animals. Recently, a type III secretion system (T3SS) has been 
      found to contribute to Ed. tarda pathogenesis. EseB, EseC and EseD were shown to 
      be secreted by the T3SS and to be the major components of the extracellular 
      proteins (ECPs). Based on sequence similarity, they have been proposed to 
      function as the 'translocon' of the T3SS needle structure. In this study, it was 
      shown that EseB, EseC and EseD formed a protein complex after secretion, which is 
      consistent with their possible roles as translocon components. The secretion of 
      EseB and EseD was dependent on EscC (previously named Orf2). EscC has the 
      characteristics of a chaperone; it is a small protein (13 kDa), located next to 
      the translocators in the T3SS gene cluster, and has a coiled-coil structure at 
      the N-terminal region as predicted by coils. An in-frame deletion of escC 
      abolished the secretion of EseB and EseD, and complementation of DeltaescC 
      restored the export of EseB and EseD into the culture supernatant. Further 
      studies showed that EscC is not a secreted protein and is located on the membrane 
      and in the cytoplasm. Mutation of escC did not affect the transcription of eseB 
      but reduced the amount of EseB as measured by using an EseB-LacZ fusion protein 
      in Ed. tarda. Co-purification studies demonstrated that EscC formed complexes 
      with EseB and EseD. The results suggest that EscC functions as a T3SS chaperone 
      for the putative translocon components EseB and EseD in Ed. tarda.
FAU - Zheng, Jun
AU  - Zheng J
AD  - Department of Biological Sciences, Faculty of Science, National University of 
      Singapore, 117543, Singapore.
FAU - Li, Nan
AU  - Li N
AD  - Department of Biological Sciences, Faculty of Science, National University of 
      Singapore, 117543, Singapore.
FAU - Tan, Yuen Peng
AU  - Tan YP
AD  - Department of Biological Sciences, Faculty of Science, National University of 
      Singapore, 117543, Singapore.
FAU - Sivaraman, J
AU  - Sivaraman J
AD  - Department of Biological Sciences, Faculty of Science, National University of 
      Singapore, 117543, Singapore.
FAU - Mok, Yu-Keung
AU  - Mok YK
AD  - Department of Biological Sciences, Faculty of Science, National University of 
      Singapore, 117543, Singapore.
FAU - Mo, Zhao Lan
AU  - Mo ZL
AD  - Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China.
FAU - Leung, Ka Yin
AU  - Leung KY
AD  - Department of Biological Sciences, Faculty of Science, National University of 
      Singapore, 117543, Singapore.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Microbiology (Reading)
JT  - Microbiology (Reading, England)
JID - 9430468
RN  - 0 (Bacterial Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Virulence Factors)
SB  - IM
MH  - Animals
MH  - Artificial Gene Fusion
MH  - Bacterial Proteins/chemistry/genetics/*metabolism
MH  - Cell Membrane/chemistry
MH  - Cytoplasm/metabolism
MH  - Edwardsiella tarda/*metabolism/pathogenicity
MH  - Enterobacteriaceae Infections/microbiology
MH  - Fish Diseases/microbiology
MH  - Gene Deletion
MH  - Gene Expression Regulation, Bacterial
MH  - Genes, Reporter
MH  - Molecular Chaperones/chemistry/genetics/*metabolism
MH  - Multiprotein Complexes
MH  - Mutagenesis, Insertional
MH  - Protein Binding
MH  - Protein Conformation
MH  - Protein Transport
MH  - Transcription, Genetic
MH  - Virulence Factors/chemistry/*metabolism
EDAT- 2007/05/29 09:00
MHDA- 2007/11/06 09:00
CRDT- 2007/05/29 09:00
PHST- 2007/05/29 09:00 [pubmed]
PHST- 2007/11/06 09:00 [medline]
PHST- 2007/05/29 09:00 [entrez]
AID - 10.1099/mic.0.2006/004952-0 [doi]
PST - ppublish
SO  - Microbiology (Reading). 2007 Jun;153(Pt 6):1953-1962. doi: 
      10.1099/mic.0.2006/004952-0.