ArticleNucleic acids research2009
The role of the conserved phenylalanine in the sigma54-interacting GAFTGA motif of bacterial enhancer binding proteins.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Engineered Phage Enables Efficient Control of Gene Expression upon Infection of the Host Cell.International journal of molecular sciences · 2024Article
- Mechanisms of DNA opening revealed in AAA+ transcription complex structures.Science advances · 2022Article
- Bacterial Enhancer Binding Proteins-AAABiomolecules · 2020Review
- Mechanisms of σJournal of molecular biology · 2019Review
- Structures of RNA Polymerase Closed and Intermediate Complexes Reveal Mechanisms of DNA Opening and Transcription Initiation.Molecular cell · 2017Article
- The bacterial enhancer-dependent RNA polymerase.The Biochemical journal · 2016Review
- Identification of the HrpS binding site in the hrpL promoter and effect of the RpoN binding site of HrpS on the regulation of the type III secretion system in Erwinia amylovora.Molecular plant pathology · 2016Article
- Genome wide interactions of wild-type and activator bypass forms of σ54.Nucleic acids research · 2015Article
- Identification of metabolism pathways directly regulated by sigma(54) factor in Bacillus thuringiensis.Frontiers in microbiology · 2015Article
- Crystallization and preliminary X-ray analysis of the ATPase domain of the σ(54)-dependent transcription activator NtrC1 from Aquifex aeolicus bound to the ATP analog ADP-BeFx.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Nucleotide-induced asymmetry within ATPase activator ring drives σ54-RNAP interaction and ATP hydrolysis.Genes & development · 2013Article
- A key hydrophobic patch identified in an AAA⁺ protein essential for its in trans inhibitory regulation.Journal of molecular biology · 2013Article
- An aromatic residue switch in enhancer-dependent bacterial RNA polymerase controls transcription intermediate complex activity.Nucleic acids research · 2013Article
- A dual switch controls bacterial enhancer-dependent transcription.Nucleic acids research · 2012Article
- A common feature from different subunits of a homomeric AAA+ protein contacts three spatially distinct transcription elements.Nucleic acids research · 2012Article
- Engineering of Rhodococcus cell catalysts for tolerance improvement by sigma factor mutation and active plasmid partition.Journal of industrial microbiology & biotechnology · 2012Article
- The role of bacterial enhancer binding proteins as specialized activators of σ54-dependent transcription.Microbiology and molecular biology reviews : MMBR · 2012Review
- Formation of MgF3 (-)-dependent complexes between an AAA(+) ATPase and σ(54.).FEBS open bio · 2012Article
- Comparative analyses imply that the enigmatic Sigma factor 54 is a central controller of the bacterial exterior.BMC genomics · 2011Article
- Regulation of type VI secretion gene clusters by sigma54 and cognate enhancer binding proteins.Journal of bacteriology · 2011Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
sigma(54)-dependent transcription requires activation by bacterial enhancer binding proteins (bEBPs). bEBPs are members of the AAA+ (ATPases associated with various cellular activities) protein family and typically form hexameric structures that are crucial for their ATPase activity. The precise mechanism by which the energy derived from ATP hydrolysis is coupled to biological output has several unknowns. Here we use Escherichia coli PspF, a model bEBP involved in the transcription of stress response genes (psp operon), to study determinants of its contact features with the closed promoter complex. We demonstrate that substitution of a highly conserved phenylalanine (F85) residue within the L1 loop GAFTGA motif affects (i) the ATP hydrolysis rate of PspF, demonstrating the link between L1 and the nucleotide binding pocket; (ii) the internal organization of the hexameric ring; and (iii) sigma(54) interactions. Importantly, we provide evidence for a close relationship between F85 and the -12 DNA fork junction structure, which may contribute to key interactions during the energy coupling step and the subsequent remodelling of the Esigma(54) closed complex. The functionality of F85 is distinct from that of other GAFTGA residues, especially T86 where in contrast to F85 a clean uncoupling phenotype is observed.
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