Phage HK022 Nun Protein Arrests Transcription on Phage λ DNA and Competes with the Phage λ N Antitermination Protein (original) (raw)
Escherichia coli NusA is required for efficient RNA binding by phage HK022 Nun protein
Randolph Watnick
Proceedings of the National Academy of Sciences, 1998
View PDFchevron_right
Control of transcription processivity in phage lambda: Nus factors strengthen the termination-resistant state of RNA polymerase induced by N antiterminator
Asis Das
Proceedings of the National Academy of Sciences, 1994
View PDFchevron_right
Transcription antitermination in vitro by lambda N gene product: Requirement for a phage nut site and the products of host nusA, nusB, and nusE genes
Asis Das
Cell, 1984
View PDFchevron_right
nusB: a protein factor necessary for transcription antitermination in vitro by phage lambda N gene product
Asis Das
Proceedings of the National Academy of Sciences, 1984
View PDFchevron_right
Interaction between the phage HK022 Nun protein and the nut RNA of phage lambda
Asis Das
Proceedings of the National Academy of Sciences, 1995
View PDFchevron_right
The Structure of the Coliphage HK022 Nun Protein-lambda -phage boxB RNA Complex. IMPLICATIONS FOR THE MECHANISM OF TRANSCRIPTION TERMINATION
Cornelius Faber
Journal of Biological Chemistry, 2001
View PDFchevron_right
Escherichia coli nusG mutations that block transcription termination by coliphage HK022 Nun protein
Siu Chun Hung
Molecular Microbiology, 1999
View PDFchevron_right
Bacteriophage lambda N protein alone can induce transcription antitermination in vitro
Asis Das
Proceedings of the National Academy of Sciences, 1996
View PDFchevron_right
The Nun protein of bacteriophage HK022 inhibits translocation of Escherichia coli RNA polymerase without abolishing its catalytic activities
Siu Chun Hung
Genes & Development, 1997
View PDFchevron_right
Fine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antitermination
Paul Rosch
Nucleic Acids Research, 2010
View PDFchevron_right
Evidence that ribosomal protein SlO itself is a cellular component necessary for transcription antitermination by phage
Krystyna Wolska
View PDFchevron_right
Probing the structure of Nun transcription arrest factor bound to RNA polymerase
Arkady Mustaev
Proceedings of the National Academy of Sciences
View PDFchevron_right
NusA protein is necessary and sufficient in vitro for phage lambda N gene product to suppress a rho-independent terminator placed downstream of nutL
Asis Das
Proceedings of the National Academy of Sciences, 1988
View PDFchevron_right
Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda
Jaime García-Mena
Proceedings of the National Academy of Sciences, 1995
View PDFchevron_right
Evidence that ribosomal protein S10 itself is a cellular component necessary for transcription antitermination by phage lambda N protein
Asis Das
Proceedings of the National Academy of Sciences, 1985
View PDFchevron_right
Formation of termination-resistant transcription complex at phage lambda nut locus: effects of altered translation and a ribosomal mutation
Asis Das
Proceedings of the National Academy of Sciences, 1984
View PDFchevron_right
Coliphage λnutL−: A unique class of mutants defective in the site of gene N product utilization for antitermination of leftward transcription
John Salstrom
Journal of Molecular Biology, 1978
View PDFchevron_right
λ nutR mutations convert HK022 nun protein from a transcription termination factor to a suppressor of termination
Renato Robledo
Journal of Molecular Biology, 1990
View PDFchevron_right
The carboxyl terminus of phage HK022 Nun includes a novel zinc-binding motif and a tryptophan required for transcription termination
Randolph Watnick
Genes & Development, 2000
View PDFchevron_right
Assembly of the N-dependent antitermination complex of phage λ: NusA and RNA bind independently to different unfolded domains of the N protein
Peter Von Hipel
Journal of Molecular Biology, 1997
View PDFchevron_right
A novel phage-encoded transcription antiterminator acts by suppressing bacterial RNA polymerase pausing
Konstantin Severinov
Nucleic Acids Research, 2012
View PDFchevron_right
Genetic analysis of bacteriophage ?N-dependent antitermination suggests a possible role for the RNA polymerase ? subunit in facilitating specific functions of NusA and NusE
Grzegorz Węgrzyn
Archives of Microbiology, 2003
View PDFchevron_right
RNA-binding specificity of E. coli NusA
Paul Rosch
Nucleic Acids Research, 2009
View PDFchevron_right
Structural basis of transcription arrest by coliphage HK022 Nun in an Escherichia coli RNA polymerase elongation complex
Arkady Mustaev
eLife, 2017
View PDFchevron_right
An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch
Klaas Hallenga
Genes & Development, 1997
View PDFchevron_right
Antitermination of E. coli rRNA transcription is caused by a control region segment containing lambda nut-like sequences
Suzanne Li
Cell, 1984
View PDFchevron_right
Transcription antitermination by phage lambda gene Q protein requires a DNA segment spanning the RNA start site
Craig Hart
Genes & Development, 1987
View PDFchevron_right
The Interaction Surface of a Bacterial Transcription Elongation Factor Required for Complex Formation with an Antiterminator during Transcription Antitermination
Ranjan Sen
Journal of Biological Chemistry, 2013
View PDFchevron_right
Independent Ligand-Induced Folding of the RNA-Binding Domain and Two Functionally Distinct Antitermination Regions in the Phage λ N Protein
Joyce Li
Molecular Cell, 1998
View PDFchevron_right
The antiterminator RNA of phage HK022
Sarbani Maiti
Journal of Molecular Biology, 1997
View PDFchevron_right
Escherichia coli RNA Polymerase Mutations Located Near the Upstream Edge of an RNA:DNA Hybrid and the Beginning of the RNA-exit Channel are Defective for Transcription Antitermination by the N Protein from Lambdoid Phage H-19B
Irfan Bandey
Journal of Molecular Biology, 2005
View PDFchevron_right
A Transcription Antiterminator Constructs a NusA-Dependent Shield to the Emerging Transcript
Asma Hatoum
Molecular Cell, 2007
View PDFchevron_right