Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351

2011 ◽  
Vol 79 (7) ◽  
pp. 2352-2357 ◽  
Author(s):  
Anna L. Stamp ◽  
Paul Owen ◽  
Kamel El Omari ◽  
Michael Lockyer ◽  
Heather K. Lamb ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Binding Protein ◽  
Structural Basis ◽  
Periplasmic Binding Protein ◽  
Serovar Typhimurium

scholarly journals FimY of Salmonella enterica serovar Typhimurium functions as a DNA-binding protein and binds the fimZ promoter

2014 ◽  
Vol 169 (7-8) ◽  
pp. 496-503 ◽  
Author(s):  
Ke-Chuan Wang ◽  
Yuan-Hsun Hsu ◽  
Yi-Ning Huang ◽  
Jiunn-Horng Lin ◽  
Kuang-Sheng Yeh
Keyword(s):  
Dna Binding ◽  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Serovar Typhimurium

scholarly journals The Amino Terminus of Salmonella enterica Serovar Typhimurium ς54 Is Required for Interactions with an Enhancer-Binding Protein and Binding to Fork Junction DNA

2000 ◽  
Vol 182 (2) ◽  
pp. 513-517 ◽  
Author(s):  
Mary T. Kelly ◽  
Timothy R. Hoover
Keyword(s):  
Salmonella Enterica ◽  
Transcription Initiation ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Binding Protein ◽  
Cross Linking ◽  
Amino Terminal ◽  
Enhancer Binding Protein ◽  
Region I ◽  
Serovar Typhimurium ◽  
Rna Polymerase Holoenzyme

ABSTRACT Transcription initiation by the ς54-RNA polymerase holoenzyme requires an enhancer-binding protein that is thought to contact ς54 to activate transcription. To identify potential enhancer-binding protein contact sites in ς54, we compared the abilities of wild-type and truncated forms ofSalmonella enterica serovar Typhimurium ς54to interact with the enhancer-binding protein DctD in a chemical cross-linking assay. Removal of two regions in the amino-terminal portion of ς54, residues 57 to 105 and residues 144 to 179, prevented cross-linking, but removal of either region alone did not. In addition, deletion of 56 amino-terminal residues of ς54 (region I) reduced the affinity of the protein for a fork junction DNA probe.

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