Structure—Function Relationships of EcDOS, a Heme-Regulated Phosphodiesterase from Escherichia coli

ChemInform ◽  
2006 ◽  
Vol 37 (19) ◽  
Author(s):  
Yukie Sasakura ◽  
Tokiko Yoshimura-Suzuki ◽  
Hirofumi Kurokawa ◽  
Toru Shimizu
Keyword(s):  
Escherichia Coli ◽  
Structure Function

scholarly journals A Rhodobacter sphaeroides Protein Mechanistically Similar to Escherichia coli DksA Regulates Photosynthetic Growth

mBio ◽  
2014 ◽  
Vol 5 (3) ◽  
Author(s):  
Christopher W. Lennon ◽  
Kimberly C. Lemmer ◽  
Jessica L. Irons ◽  
Max I. Sellman ◽  
Timothy J. Donohue ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structure Function ◽  
Rhodobacter Sphaeroides ◽  
Fatty Acid Content ◽  
Regulatory Protein ◽  
Growth Conditions ◽  
Globular Domain ◽  
Content Type ◽  
E Coli

ABSTRACTDksA is a global regulatory protein that, together with the alarmone ppGpp, is required for the “stringent response” to nutrient starvation in the gammaproteobacteriumEscherichia coliand for more moderate shifts between growth conditions. DksA modulates the expression of hundreds of genes, directly or indirectly. Mutants lacking a DksA homolog exhibit pleiotropic phenotypes in other gammaproteobacteria as well. Here we analyzed the DksA homolog RSP2654 in the more distantly relatedRhodobacter sphaeroides, an alphaproteobacterium. RSP2654 is 42% identical and similar in length toE. coliDksA but lacks the Zn finger motif of theE. coliDksA globular domain. Deletion of the RSP2654 gene results in defects in photosynthetic growth, impaired utilization of amino acids, and an increase in fatty acid content. RSP2654 complements the growth and regulatory defects of anE. colistrain lacking thedksAgene and modulates transcriptionin vitrowithE. coliRNA polymerase (RNAP) similarly toE. coliDksA. RSP2654 reduces RNAP-promoter complex stabilityin vitrowith RNAPs fromE. coliorR. sphaeroides, alone and synergistically with ppGpp, suggesting that even though it has limited sequence identity toE. coliDksA (DksAEc), it functions in a mechanistically similar manner. We therefore designate the RSP2654 protein DksARsp. Our work suggests that DksARsphas distinct and important physiological roles in alphaproteobacteria and will be useful for understanding structure-function relationships in DksA and the mechanism of synergy between DksA and ppGpp.IMPORTANCEThe role of DksA has been analyzed primarily in the gammaproteobacteria, in which it is best understood for its role in control of the synthesis of the translation apparatus and amino acid biosynthesis. Our work suggests that DksA plays distinct and important physiological roles in alphaproteobacteria, including the control of photosynthesis inRhodobacter sphaeroides. The study of DksARsp, should be useful for understanding structure-function relationships in the protein, including those that play a role in the little-understood synergy between DksA and ppGpp.

scholarly journals Using Structure-Function Relationships to Understand the Mechanism of Phenazine Mediated Extracellular Electron Transfer in Escherichia coli

iScience ◽  
2021 ◽  
pp. 103033
Author(s):  
Zayn Rhodes ◽  
Olja Simoska ◽  
Ashwini Dantanarayana ◽  
Keith J. Stevenson ◽  
Shelley D. Minteer
Keyword(s):  
Escherichia Coli ◽  
Electron Transfer ◽  
Structure Function ◽  
Extracellular Electron Transfer

Structure-function studies of the large subunit of ribonucleotide reductase from Escherichia coli

1988 ◽  
Vol 16 (2) ◽  
pp. 91-94 ◽  
Author(s):  
OLLE NILSSON ◽  
TOMAS LUNDQVIST ◽  
SOLVEIG HAHNE ◽  
BRITT-MARIE SJÖBERG
Keyword(s):  
Escherichia Coli ◽  
Structure Function ◽  
Ribonucleotide Reductase ◽  
Large Subunit

New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli

FEBS Journal ◽  
2010 ◽  
Vol 277 (12) ◽  
pp. 2628-2640 ◽  
Author(s):  
Tobias Werther ◽  
Agnes Zimmer ◽  
Georg Wille ◽  
Ralph Golbik ◽  
Manfred S. Weiss ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structure Function
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