Structural Basis for Promoter −10 Element Recognition by the Bacterial RNA Polymerase σ Subunit | Zendy

Andrey Feklístov | Zendy; Seth A. Darst | Zendy

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Structural Basis for Promoter −10 Element Recognition by the Bacterial RNA Polymerase σ Subunit

Author(s) -

Andrey Feklístov,

Seth A. Darst

Publication year - 2011

Publication title -

cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 26.304

H-Index - 776

eISSN - 1097-4172

pISSN - 0092-8674

DOI - 10.1016/j.cell.2011.10.041

Subject(s) - biology , rna polymerase , transcription (linguistics) , base pair , dna , promoter , protein subunit , transcription bubble , polymerase , rna , specificity factor , microbiology and biotechnology , genetics , gene , gene expression , linguistics , philosophy

The key step in bacterial promoter opening is recognition of the -10 promoter element (T(-12)A(-11)T(-10)A(-9)A(-8)T(-7) consensus sequence) by the RNA polymerase σ subunit. We determined crystal structures of σ domain 2 bound to single-stranded DNA bearing-10 element sequences. Extensive interactions occur between the protein and the DNA backbone of every -10 element nucleotide. Base-specific interactions occur primarily with A(-11) and T(-7), which are flipped out of the single-stranded DNA base stack and buried deep in protein pockets. The structures, along with biochemical data, support a model where the recognition of the -10 element sequence drives initial promoter opening as the bases of the nontemplate strand are extruded from the DNA double-helix and captured by σ. These results provide a detailed structural basis for the critical roles of A(-11) and T(-7) in promoter melting and reveal important insights into the initiation of transcription bubble formation.

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