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Structure. 2014 Mar 4;22(3):488-95. doi: 10.1016/j.str.2013.12.010. Epub 2014 Jan 16.

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

Author information

1
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
2
Department of Genetics and Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA.
3
Department of Chemistry and Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA.
4
Center for Advanced Biotechnology and Medicine, Rutgers University, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ 08854, USA; Northeast Structural Genomics Consortium, Rutgers University, Piscataway, NJ 08854, USA.
5
Department of Chemistry and Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA. Electronic address: ebright@waksman.rutgers.edu.
6
Department of Genetics and Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA. Electronic address: bnickels@waksman.rutgers.edu.

Abstract

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 the β subunit. We present the 2.1 Å resolution crystal structure of a portion of λQ containing determinants for interaction with DNA, interaction with region 4 of σ(70), and interaction with the β 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 λQ alters the functional properties of the transcription elongation complex.

PMID:
24440517
PMCID:
PMC3951671
DOI:
10.1016/j.str.2013.12.010
[Indexed for MEDLINE]
Free PMC Article

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