Structural basis of transcription activation

Yu Feng, Yu Zhang, Richard H. Ebright

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

Abstract

Class II transcription activators function by binding to a DNA site overlapping a core promoter and stimulating isomerization of an initial RNA polymerase (RNAP)-promoter closed complex into a catalytically competent RNAP-promoter open complex. Here, we report a 4.4 angstrom crystal structure of an intact bacterial class II transcription activation complex. The structure comprises Thermus thermophilus transcription activator protein TTHB099 (TAP) [homolog of Escherichia coli catabolite activator protein (CAP)], T. thermophilus RNAP σA holoenzyme, a class II TAP-dependent promoter, and a ribotetranucleotide primer. The structure reveals the interactions between RNAP holoenzyme and DNA responsible for transcription initiation and reveals the interactions between TAP and RNAP holoenzyme responsible for transcription activation. The structure indicates that TAP stimulates isomerization through simple, adhesive, stabilizing protein-protein interactions with RNAP holoenzyme.

Original languageEnglish (US)
Pages (from-to)1330-1333
Number of pages4
JournalScience
Volume352
Issue number6291
DOIs
StatePublished - Jun 10 2016

All Science Journal Classification (ASJC) codes

  • General

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