Site-directed mutagenesis of the response regulator DmsR for the dmsCBA operon expression in Rhodobacter sphaeroides f. sp. denitrificans: an essential residue of proline-130 in the linker

1999 ◽  
Vol 1447 (1) ◽  
pp. 57-63 ◽  
Author(s):  
Isamu Yamamoto ◽  
Keiko Takamatsu ◽  
Yoshinori Ohshima ◽  
Takeshi Ujiiye ◽  
Toshio Satoh
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Response Regulator ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Operon Expression

Site-Directed Mutagenesis of Reaction Centers from Rhodobacter sphaeroides

1990 ◽  
pp. 161-164
Author(s):  
M. L. Paddock ◽  
S. H. Rongey ◽  
J. W. Farchaus ◽  
G. Feher ◽  
M. Y. Okamura
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Reaction Centers ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

Site-directed mutagenesis of substrate binding sites of azoreductase from Rhodobacter sphaeroides

2007 ◽  
Vol 30 (5) ◽  
pp. 869-875 ◽  
Author(s):  
Guangfei Liu ◽  
Jiti Zhou ◽  
Jing Wang ◽  
Bin Yan ◽  
Jingmei Li ◽  
...  
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Binding Sites ◽  
Substrate Binding ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Substrate Binding Sites

scholarly journals The SKHR Motif Is Required for Biological Function of the VirR Response Regulator from Clostridium perfringens

2003 ◽  
Vol 185 (20) ◽  
pp. 6205-6208 ◽  
Author(s):  
Sheena McGowan ◽  
Jennifer R. O'Connor ◽  
Jackie K. Cheung ◽  
Julian I. Rood
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Clostridium Perfringens ◽  
Biological Function ◽  
Response Regulator ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Toxin Gene

ABSTRACT The response regulator VirR and its cognate sensor histidine kinase, VirS, are responsible for toxin gene regulation in the human pathogen Clostridium perfringens. The C-terminal domain of VirR (VirRc) contains the functional FxRxHrS motif, which is involved in DNA binding and is conserved in many regulatory proteins. VirRc was cloned, purified, and shown by in vivo and in vitro studies to comprise an independent DNA binding domain. Random and site-directed mutagenesis was used to identify further amino acids that were required for the functional integrity of the protein. Random mutagenesis identified a unique residue, Met-172, that was required for biological function. Site-directed mutagenesis of the SKHR motif (amino acids 216 to 219) revealed that these residues were also required for biological activity. Analysis of the mutated proteins indicated that they were unable to bind to the DNA target with the same efficiency as the wild-type protein.

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