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Structure of the DNA-binding and RNA-polymerase-binding region of transcription antitermination factor ?Q.

ABSTRACT: The bacteriophage ? Q protein is a transcription antitermination factor that controls expression of the phage late genes as a stable component of the transcription elongation complex. To join the elongation complex, ?Q binds a specific DNA sequence element and interacts with RNA polymerase that is paused during early elongation. ?Q binds to the paused early-elongation complex through interactions between ?Q and two regions of RNA polymerase: region 4 of the ?(70) subunit and the flap region of the ? subunit. We present the 2.1 Å resolution crystal structure of a portion of ?Q containing determinants for interaction with DNA, interaction with region 4 of ?(70), and interaction with the ? flap. The structure provides a framework for interpreting prior genetic and biochemical analysis and sets the stage for future structural studies to elucidate the mechanism by which ?Q alters the functional properties of the transcription elongation complex.

SUBMITTER: Vorobiev SM 

PROVIDER: S-EPMC3951671 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

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Structure of the DNA-binding and RNA-polymerase-binding region of transcription antitermination factor λQ.

Vorobiev Sergey M SM   Gensler Yocheved Y   Vahedian-Movahed Hanif H   Seetharaman Jayaraman J   Su Min M   Huang Janet Y JY   Xiao Rong R   Kornhaber Gregory G   Montelione Gaetano T GT   Tong Liang L   Ebright Richard H RH   Nickels Bryce E BE  

Structure (London, England : 1993) 20140116 3

The bacteriophage λ Q protein is a transcription antitermination factor that controls expression of the phage late genes as a stable component of the transcription elongation complex. To join the elongation complex, λQ binds a specific DNA sequence element and interacts with RNA polymerase that is paused during early elongation. λQ binds to the paused early-elongation complex through interactions between λQ and two regions of RNA polymerase: region 4 of the σ(70) subunit and the flap region of t  ...[more]

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