RpoE

From SubtiWiki
Revision as of 14:06, 13 May 2013 by 134.76.70.252 (talk)
Jump to: navigation, search
  • Description: RNA polymerase delta subunit, affects the regulation of RNA polymerase by the concentration of the initiating nucleoside triphosphate ([iNTP])

Gene name rpoE
Synonyms
Essential no
Product RNA polymerase delta subunit
Function transcription
Gene expression levels in SubtiExpress: rpoE
Interactions involving this protein in SubtInteract: RpoE
Metabolic function and regulation of this protein in SubtiPathways:
Fatty acid degradation
MW, pI 20 kDa, 3.654
Gene length, protein length 519 bp, 173 aa
Immediate neighbours pyrG, acdA
Sequences Protein DNA Advanced_DNA
Genetic context
RpoE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpoE expression.png















Categories containing this gene/protein

transcription

This gene is a member of the following regulons

FadR regulon

The gene

Basic information

  • Locus tag: BSU37160

Phenotypes of a mutant

  • RpoE is essential for cell survival when facing a competing strain in changing environment PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: rpoE family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • fadF: repressed in the absence of long-chain fatty acids (FadR) PubMed
  • Regulatory mechanism:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Arthur Aronson, Purdue University, West Lafayette, USA homepage

Your additional remarks

References

Reviews

Lakshminarayan M Iyer, L Aravind
Insights from the architecture of the bacterial transcription apparatus.
J Struct Biol: 2012, 179(3);299-319
[PubMed:22210308] [WorldCat.org] [DOI] (I p)

Original publications

Alžbeta Rabatinová, Hana Šanderová, Jitka Jirát Matějčková, Jana Korelusová, Luděk Sojka, Ivan Barvík, Veronika Papoušková, Vladimír Sklenár, Lukáš Žídek, Libor Krásný
The δ subunit of RNA polymerase is required for rapid changes in gene expression and competitive fitness of the cell.
J Bacteriol: 2013, 195(11);2603-11
[PubMed:23543716] [WorldCat.org] [DOI] (I p)

Anna Zawadzka-Kazimierczuk, Wiktor Koźmiński, Hana Sanderová, Libor Krásný
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins.
J Biomol NMR: 2012, 52(4);329-37
[PubMed:22350953] [WorldCat.org] [DOI] (I p)

Jiří Nováček, Anna Zawadzka-Kazimierczuk, Veronika Papoušková, Lukáš Zídek, Hana Sanderová, Libor Krásný, Wiktor Koźmiński, Vladimír Sklenář
5D 13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion.
J Biomol NMR: 2011, 50(1);1-11
[PubMed:21424579] [WorldCat.org] [DOI] (I p)

Veronika Motáčková, Jiří Nováček, Anna Zawadzka-Kazimierczuk, Krzysztof Kazimierczuk, Lukáš Zídek, Hana Sanderová, Libor Krásný, Wiktor Koźmiński, Vladimír Sklenář
Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced 5D experiments.
J Biomol NMR: 2010, 48(3);169-77
[PubMed:20890634] [WorldCat.org] [DOI] (I p)

Geoff P Doherty, Mark J Fogg, Anthony J Wilkinson, Peter J Lewis
Small subunits of RNA polymerase: localization, levels and implications for core enzyme composition.
Microbiology (Reading): 2010, 156(Pt 12);3532-3543
[PubMed:20724389] [WorldCat.org] [DOI] (I p)

Veronika Motácková, Hana Sanderová, Lukás Zídek, Jirí Novácek, Petr Padrta, Alzbeta Svenková, Jana Korelusová, Jirí Jonák, Libor Krásný, Vladimír Sklenár
Solution structure of the N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase and its classification based on structural homologs.
Proteins: 2010, 78(7);1807-10
[PubMed:20310067] [WorldCat.org] [DOI] (I p)

Hiroshi Matsuoka, Kazutake Hirooka, Yasutaro Fujita
Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation.
J Biol Chem: 2007, 282(8);5180-94
[PubMed:17189250] [WorldCat.org] [DOI] (P p)

F J López de Saro, N Yoshikawa, J D Helmann
Expression, abundance, and RNA polymerase binding properties of the delta factor of Bacillus subtilis.
J Biol Chem: 1999, 274(22);15953-8
[PubMed:10336502] [WorldCat.org] [DOI] (P p)

F J López de Saro, A Y Woody, J D Helmann
Structural analysis of the Bacillus subtilis delta factor: a protein polyanion which displaces RNA from RNA polymerase.
J Mol Biol: 1995, 252(2);189-202
[PubMed:7545758] [WorldCat.org] [DOI] (P p)

Y L Juang, J D Helmann
Pathway of promoter melting by Bacillus subtilis RNA polymerase at a stable RNA promoter: effects of temperature, delta protein, and sigma factor mutations.
Biochemistry: 1995, 34(26);8465-73
[PubMed:7599136] [WorldCat.org] [DOI] (P p)

Y L Juang, J D Helmann
The delta subunit of Bacillus subtilis RNA polymerase. An allosteric effector of the initiation and core-recycling phases of transcription.
J Mol Biol: 1994, 239(1);1-14
[PubMed:7515111] [WorldCat.org] [DOI] (P p)

M Lampe, C Binnie, R Schmidt, R Losick
Cloned gene encoding the delta subunit of Bacillus subtilis RNA polymerase.
Gene: 1988, 67(1);13-9
[PubMed:2843435] [WorldCat.org] [DOI] (P p)

E I Hyde, M D Hilton, H R Whiteley
Interactions of Bacillus subtilis RNA polymerase with subunits determining the specificity of initiation. Sigma and delta peptides can bind simultaneously to core.
J Biol Chem: 1986, 261(35);16565-70
[PubMed:3097010] [WorldCat.org] (P p)

E C Achberger, H R Whiteley
The role of the delta peptide of the Bacillus subtilis RNA polymerase in promoter selection.
J Biol Chem: 1981, 256(14);7424-32
[PubMed:6788769] [WorldCat.org] (P p)