Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of dual activation of cell division by the actinobacterial transcription factors WhiA and WhiB.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 120, Issue 11, Page e2220785120, Year 2023
Publish date	Mar 14, 2023
Authors	Mirjana Lilic / Neil A Holmes / Matthew J Bush / Alexandra K Marti / David A Widdick / Kim C Findlay / Young Joo Choi / Ruby Froom / Steven Koh / Mark J Buttner / Elizabeth A Campbell /
PubMed Abstract	Studies of transcriptional initiation in different bacterial clades reveal diverse molecular mechanisms regulating this first step in gene expression. The WhiA and WhiB factors are both required to ...Studies of transcriptional initiation in different bacterial clades reveal diverse molecular mechanisms regulating this first step in gene expression. The WhiA and WhiB factors are both required to express cell division genes in Actinobacteria and are essential in notable pathogens such as . The WhiA/B regulons and binding sites have been elucidated in (), where they coordinate to activate sporulation septation. However, how these factors cooperate at the molecular level is not understood. Here we present cryoelectron microscopy structures of transcriptional regulatory complexes comprising RNA polymerase (RNAP) σ-holoenzyme and WhiA and WhiB, in complex with the WhiA/B target promoter . These structures reveal that WhiB binds to domain 4 of σ (σ) of the σ-holoenzyme, bridging an interaction with WhiA while making non-specific contacts with the DNA upstream of the -35 core promoter element. The N-terminal homing endonuclease-like domain of WhiA interacts with WhiB, while the WhiA C-terminal domain (WhiA-CTD) makes base-specific contacts with the conserved WhiA GACAC motif. Notably, the structure of the WhiA-CTD and its interactions with the WhiA motif are strikingly similar to those observed between σ housekeeping σ-factors and the -35 promoter element, suggesting an evolutionary relationship. Structure-guided mutagenesis designed to disrupt these protein-DNA interactions reduces or abolishes developmental cell division in confirming their significance. Finally, we compare the architecture of the WhiA/B σ-holoenzyme promoter complex with the unrelated but model CAP Class I and Class II complexes, showing that WhiA/WhiB represent a new mechanism in bacterial transcriptional activation.
External links	Proc Natl Acad Sci U S A / PubMed:36888660 / PubMed Central
Methods	EM (single particle)
Resolution	3.12 - 3.18 Å
Structure data	27777 8dy7 EMDB-27777, PDB-8dy7: Streptomyces venezuelae RNAP transcription open promoter complex with WhiA and WhiB transcription factors Method: EM (single particle) / Resolution: 3.18 Å 27778 8dy9 EMDB-27778, PDB-8dy9: Streptomyces venezuelae RNAP unconstrained open promoter complex with WhiA and WhiB transcription factors Method: EM (single particle) / Resolution: 3.12 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry ChemComp-SF4: IRON/SULFUR CLUSTER / Iron–sulfur cluster
Source	streptomyces venezuelae (bacteria) streptomyces venezuelae atcc 10712 (bacteria)
Keywords	TRANSCRIPTION/TRANSFERASE/DNA / RNA polymerase / Transcription factor / Iron cluster / TRANSCRIPTION-TRANSFERASE-DNA complex