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TitleStructural basis of σ appropriation.
Journal, issue, pagesNucleic Acids Res., Year 2019
Publish dateAug 8, 2019
AuthorsJing Shi / Aijia Wen / Minxing Zhao / Linlin You / Yu Zhang / Yu Feng /
PubMed AbstractBacteriophage T4 middle promoters are activated through a process called σ appropriation, which requires the concerted effort of two T4-encoded transcription factors: AsiA and MotA. Despite ...Bacteriophage T4 middle promoters are activated through a process called σ appropriation, which requires the concerted effort of two T4-encoded transcription factors: AsiA and MotA. Despite extensive biochemical and genetic analyses, puzzle remains, in part, because of a lack of precise structural information for σ appropriation complex. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact σ appropriation complex, comprising AsiA, MotA, Escherichia coli RNA polymerase (RNAP), σ70 and a T4 middle promoter. As expected, AsiA binds to and remodels σ region 4 to prevent its contact with host promoters. Unexpectedly, AsiA undergoes a large conformational change, takes over the job of σ region 4 and provides an anchor point for the upstream double-stranded DNA. Because σ region 4 is conserved among bacteria, other transcription factors may use the same strategy to alter the landscape of transcription immediately. Together, the structure provides a foundation for understanding σ appropriation and transcription activation.
External linksPubMed:31392983 / Publisher's page
KeywordsTRANSCRIPTION / RNA polymerase / sigma appropriation / transcription activation / promoter
MethodsEM (single particle)
Resolution3.79 A
Structure data

EMDB-9916:
CryoEM structure of sigma appropriation complex

PDB-6k4y:
CryoEM structure of sigma appropriation complex

Chemicals

ChemComp-MG:
MAGNESIUM IONMagnesium

ChemComp-ZN:
ZINC IONZinc

Source
  • escherichia coli k-12 (bacteria)
  • enterobacteria phage t4 (bacteriophage)

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