Structural Basis of Response Regulator Inhibition by a Bacterial Anti-Activator Protein | Zendy

Melinda D. Baker | Zendy; Matthew B. Neiditch | Zendy

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Structural Basis of Response Regulator Inhibition by a Bacterial Anti-Activator Protein

Author(s) -

Melinda D. Baker,

Matthew B. Neiditch

Publication year - 2011

Publication title -

plos biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 4.127

H-Index - 271

eISSN - 1545-7885

pISSN - 1544-9173

DOI - 10.1371/journal.pbio.1001226

Subject(s) - biology , activator (genetics) , regulator , microbiology and biotechnology , bacillus subtilis , promoter , dna , dna binding domain , biochemistry , genetics , gene , transcription factor , gene expression , bacteria

Structure-function studies reveal that Rap proteins have distinct, nonoverlapping surfaces that interact with different cellular targets, and that for antiactivator RapF, one surface mimics DNA to bind a response regulator DNA binding domain, thereby sterically preventing the activity of this transcription transactivator.

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