RNA polymerase delta subunit, affects the regulation of RNA polymerase by the concentration of the initiating nucleoside triphosphate (iNTP)
product
RNA polymerase delta subunit
Genomic Context
categories
[category|SW 3|Information processing] → [category|SW 3.2|RNA synthesis and degradation] → [category|SW 3.2.1|Transcription] → [category|SW 3.2.1.1|RNA polymerase][SW|Categories] containing this gene/protein
[SW|transcription]This gene is a member of the following [SW|regulons]
[SW|FadR regulon]Gene
Coordinates on the chromosome (coding sequence)
3,812,542 -> 3,813,063
Phenotypes of a mutant
[protein|search|RpoE] is essential for cell survival when facing a competing strain in changing environment [Pubmed|23543716]The protein
Catalyzed reaction/ biological activity
binds to DNA immediately upstream of the promoter element at A-rich sequences on the abrB and rrnB1 promoters and facilitates open complex formation [Pubmed|26546673]Protein family
rpoE family (according to Swiss-Prot)Structure
[PDB|2M4K] (full-length protein) [Pubmed|23868186][PDB|2KRC] (N-terminal domain) [Pubmed|20310067][SW|Localization]
closely associated with [SW|RNA polymerase] involved in transcribing both mRNA and rRNA operons [Pubmed|20724389][SW|Interactions]
closely associated to [SW|RNA polymerase] ([protein|search|RpoA](2)-[protein|search|RpoB]-[protein|search|RpoC]) [Pubmed|20724389]associates only to the core [SW|RNA polymerase], not to the holoenzyme [Pubmed|26546673][protein|search|RpoB]-[protein|search|RpoE] (demonstrated for ''S. aureus'') [Pubmed|24491578][protein|search|RpoC]-[protein|search|RpoE] (demonstrated for ''S. aureus'') [Pubmed|24491578]Expression and Regulation
Operon
''[protein|search|fadF]-[protein|search|acdA]-[protein|search|rpoE]'' [Pubmed|17189250]''[protein|search|rpoE]'' [Pubmed|10336502][SW|Sigma factor]
''[protein|search|fadF]'': [protein|search|SigA] [Pubmed|17189250]''[protein|search|rpoE]'': [protein|search|SigA] [Pubmed|10336502]Regulation
''[protein|search|fadF]'': repressed in the absence of long-chain fatty acids ([protein|search|FadR]) [Pubmed|17189250]Regulatory mechanism
[protein|search|FadR]: transcription repression [Pubmed|17189250]Additional information
present at equimolar levels with [[RNA polymerase]] [PubMed|20724389]Labs working on this gene/protein
[SW|Arthur Aronson], Purdue University, West Lafayette, USA [http://wwwdev.gradschool.purdue.edu/PULSe/faculty.cfm?fid=5&range=0 homepage]References
Reviews
Original publications
7545758,7599136,7515111,10336502,2843435,17189250,3097010,6788769,23543716,22350953,20890634,20724389,20310067,23868186,21424579,24520113,24937760,24491578,26546673 
