The N-acetyltransferase RimJ responds to environmental stimuli to repress pap fimbrial transcription in Escherichia coli.
In uropathogenic Escherichia coli, P pili (Pap) facilitate binding to host epithelial cells and subsequent colonization. Whereas P pili can be produced at 37 degrees C, the expression of these fimbriae is suppressed at 23 degrees C. Previously, insertion mutations in rimJ, a gene encoding the N-terminal acetyltransferase of ribosomal protein S5, were shown to disrupt this thermoregulatory response, allowing papBA transcription at low temperature. In this study, we created an in-frame deletion of rimJ. This deletion relieved the repressive effects not only of low temperature but also of rich (Luria-Bertani [LB]) medium and glucose on papBA transcription, indicating that RimJ modulates papBA transcription in response to multiple environmental stimuli. papI transcription was also shown to be regulated by RimJ. papBA transcription is also controlled by a phase variation mechanism. We demonstrated that the regulators necessary to establish a phase ON state--PapI, PapB, Dam, Lrp, and cyclic AMP-CAP-are still required for papBA transcription in a rimJ mutant strain. rimJ mutations increase the rate at which bacteria transition into the phase ON state, indicating that RimJ inhibits the phase OFF-->ON transition. A DeltarimJ hns651 mutant is viable on LB medium but not on minimal medium. This synthetic lethality, along with transcriptional analyses, indicates that RimJ and H-NS work through separate pathways to control papBA transcription. Mutations in rimJ do not greatly influence the transcription of the fan, daa, or fim operon, suggesting that RimJ may be a pap-specific regulator. Overexpression of rimJ under conditions repressive for papBA transcription complements the DeltarimJ mutation but has little effect on transcription under activating conditions, indicating that the ability of RimJ to regulate transcription is environmentally controlled.
White-Ziegler
Christine A
CA
Department of Biological Sciences, Smith College, Northampton, Massachusetts 01063, USA. cwhitezi@science.smith.edu.
Black
Alia M
AM
Eliades
Stacie H
SH
Young
Sarah
S
Porter
Kimberly
K
D000123:Acetyltransferases; D001191:Arylamine N-Acetyltransferase / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D001833:Body Temperature Regulation / Q000235:genetics; D000242:Cyclic AMP / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D004777:Environment; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000235:genetics*; D017353:Gene Deletion; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D051756:Leucine-Responsive Regulatory Protein; D008565:Membrane Proteins; D016296:Mutagenesis / Q000502:physiology; D011953:Receptors, Cyclic AMP / Q000378:metabolism; D012097:Repressor Proteins; D012269:Ribosomal Proteins / Q000235:genetics* / Q000378:metabolism; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific) / Q000378:metabolism; D013696:Temperature; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic / Q000502:physiology*
C078802:AtpA protein, E coli; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C080953:DaaA protein, E coli; D029968:Escherichia coli Proteins; C107309:FanA protein, E coli; C031908:H-NS protein, bacteria; C497278:Lrp protein, E coli; D008565:Membrane Proteins; C086707:PapI protein, E coli; D011953:Receptors, Cyclic AMP; D012097:Repressor Proteins; D012269:Ribosomal Proteins; D014157:Transcription Factors; C116245:atpD protein, E coli; C063055:fimbrillin; C077567:RimJ protein, E coli; D051756:Leucine-Responsive Regulatory Protein; D036781:Fimbriae Proteins; D000242:Cyclic AMP; C058693:Dam methyltransferase; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific); C499294:dam protein, E coli; D000123:Acetyltransferases; D001191:Arylamine N-Acetyltransferase