Structure of the DNA-binding and RNA-polymerase-binding region of transcription antitermination factor λQ.
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.
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
Sergey M
SM
Vorobiev
Department of Genetics and Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA.
Yocheved
Y
Gensler
Department of Chemistry and Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA.
Hanif
H
Vahedian-Movahed
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
Jayaraman
J
Seetharaman
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
Min
M
Su
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.
Janet Y
JY
Huang
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.
Rong
R
Xiao
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.
Gregory
G
Kornhaber
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.
Gaetano T
GT
Montelione
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
Liang
L
Tong
Department of Chemistry and Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA. Electronic address: ebright@waksman.rutgers.edu.
Richard H
RH
Ebright
Department of Genetics and Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA. Electronic address: bnickels@waksman.rutgers.edu.
Bryce E
BE
Nickels
D001665:Binding Sites; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism
C066119:Q protein, Bacteriophage lambda; D014764:Viral Proteins; D004247:DNA; D012321:DNA-Directed RNA Polymerases; D015032:Zinc