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

Journal Article · · mBio (Online)
 [1];  [2];  [3];  [2];  [4];  [3];  [3]
  1. Univ. of Wisconsin, Madison, WI (United States). Dept. of Bacteriology; DOE/OSTI
  2. Univ. of Wisconsin, Madison, WI (United States). Wisconsin Energy Inst. DOE Great Lakes Bioenergy Research Center
  3. Univ. of Wisconsin, Madison, WI (United States). Dept. of Bacteriology
  4. Univ. of Wisconsin, Madison, WI (United States). Dept. of Bacteriology; Univ. of Wisconsin, Madison, WI (United States). Wisconsin Energy Inst. DOE Great Lakes Bioenergy Research Center
DksA is a global regulatory protein that, together with the alarmone ppGpp, is required for the “stringent response” to nutrient starvation in the gammaproteobacterium Escherichia coli and 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 related Rhodobacter sphaeroides, an alphaproteobacterium. RSP2654 is 42% identical and similar in length to E. coli DksA but lacks the Zn finger motif of the E. coli DksA 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 an E. coli strain lacking the dksA gene and modulates transcription in vitro with E. coli RNA polymerase (RNAP) similarly to E. coli DksA. RSP2654 reduces RNAP-promoter complex stability in vitro with RNAPs from E. coli or R. sphaeroides, alone and synergistically with ppGpp, suggesting that even though it has limited sequence identity to E. coli DksA (DksAEc), it functions in a mechanistically similar manner. We therefore designate the RSP2654 protein DksARsp. Our work suggests that DksARsp has 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.
Research Organization:
Univ. of Wisconsin, Madison, WI (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
Grant/Contract Number:
FC02-07ER64494
OSTI ID:
1626127
Journal Information:
mBio (Online), Journal Name: mBio (Online) Journal Issue: 3 Vol. 5; ISSN 2150-7511
Publisher:
American Society for Microbiology (ASM)Copyright Statement
Country of Publication:
United States
Language:
English

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