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. 2001 Feb;183(4):1452-4.
doi: 10.1128/JB.183.4.1452-1454.2001.

SigE is a chaperone for the Salmonella enterica serovar Typhimurium invasion protein SigD

K H Darwin  1 , L S Robinson, V L Miller
Affiliations

SigE is a chaperone for the Salmonella enterica serovar Typhimurium invasion protein SigD

K H Darwin et al. J Bacteriol. 2001 Feb.

Abstract

SigD is translocated into eucaryotic cells by a type III secretion system. In this work, evidence that the putative chaperone SigE directly interacts with SigD is presented. A bacterial two-hybrid system demonstrated that SigE can interact with itself and SigD. In addition, SigD was specifically copurified with SigE-His(6) on a nickel column.

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Figures

FIG. 1
FIG. 1
Immunoblot analysis using polyclonal antibodies directed against SigD (amino acids 1 to 192) of proteins from 14028s (wild type), SVM167 (sigE::Tn10dTc), SVM167 pWKS30 (vector), SVM167 pHH26 (pWSK29-sigE), SVM255 (sigD), SVM167 pHH10 (sigDE+), and pHH10-23 (sigD+) strains.
FIG. 2
FIG. 2
SigD copurifies with SigE-His6. (A) Coomassie brilliant blue-stained 12.5% polyacrylamide gel of fractions eluted from a nickel-agarose column. Positions of molecular mass standards (MW) are indicated on the left in kilodaltons. Lane S, soluble fraction after sonication of cell pellets and removal of insoluble debris by centrifugation; lanes 1 to 5, imidazole-eluted fractions. (B) Immunoblot analysis of the same fractions using antibodies to SigD or SigE. The major band labeled SicA-6XHis in panel A was confirmed to be SicA by antibodies specific to SicA (data not shown).
See this image and copyright information in PMC

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