Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Siva R. Wigneshweraraj"'
Autor:
Carol Sheppard, Beatriz Cámara, Andrey Shadrin, Natalia Akulenko, Minhao Liu, Geoff Baldwin, Konstantin Severinov, Ernesto Cota, Steve Matthews, Siva R Wigneshweraraj
Publikováno v:
Journal of Molecular Biology. 412:832-841
Gp2, a 7 kDa protein encoded by T7 bacteriophage, is a potent inhibitor of Escherichia coli RNA polymerase (RNAp), the enzyme responsible for transcription of all bacterial genes and early viral genes. A prominent feature in the structure of Gp2 is a
Autor:
Beatriz Cámara, Xiaodong Zhang, Patricia C. Burrows, B. Tracy Nixon, Kathleen Dawes, Mathieu Rappas, Martin Buck, Wendy Cannon, Siva R. Wigneshweraraj, Nicolas Joly
Publikováno v:
Journal of Molecular Biology. 387:306-319
ATP-driven remodelling of initial RNA polymerase (RNAP) promoter complexes occurs as a major post recruitment strategy used to control gene expression. Using a model-enhancer-dependent bacterial system (sigma54-RNAP, Esigma54) and a slowly hydrolysed
Autor:
Xiaodong Zhang, Martin Buck, Mathieu Rappas, Patricia C. Burrows, Tillmann Pape, Daniel Bose, Siva R. Wigneshweraraj
Publikováno v:
Molecular Cell
Transcription initiation involves the conversion from closed promoter complexes, comprising RNA polymerase (RNAP) and double-stranded promoter DNA, to open complexes, in which the enzyme is able to access the DNA template in a single-stranded form. T
Publikováno v:
Journal of Molecular Biology. 359:1182-1195
The bacterial RNA polymerase (RNAP) is a multi-subunit, structurally flexible, complex molecular machine, in which activities associated with DNA opening for transcription-competent open promoter complex (OC) formation reside in the catalytic beta an
Autor:
Sergei Nechaev, Siva R. Wigneshweraraj, Martin Buck, Patricia C. Burrows, Konstantin Severinov, Nikolay Zenkin
Publikováno v:
The EMBO Journal. 23:4264-4274
We used bacteriophage T7-encoded transcription inhibitor gene protein 2 (gp2) as a probe to study the contribution of the Escherichia coli RNA polymerase (RNAP) beta' subunit jaw domain--the site of gp2 binding--to activator and ATP hydrolysis-depend
Autor:
Matthew Chaney, Siva R. Wigneshweraraj, Angel Ernesto Dago, Patricia Bordes, Martin Buck, Enrique Morett
Publikováno v:
Molecular Microbiology. 54:489-506
Conversion of Esigma(54) closed promoter complexes to open promoter complexes requires specialized activators which are members of the AAA (ATPases Associated with various cellular Activities) protein family. The ATP binding and hydrolysis activity o
Autor:
Patricia C. Burrows, Siva R. Wigneshweraraj, Konstantin Severinov, Martin Buck, Akira Ishihama
Publikováno v:
Journal of Biological Chemistry. 278:29728-29743
The sigma 54 promoter specificity factor is distinct from sigma 70-type factors. The sigma 54-RNA polymerase binds to promoters with conserved sequence elements at -24 and -12 and utilizes specialized enhancer-binding activators to convert, through a
Autor:
Xiaodong Zhang, Matthew Chaney, Jörg Schumacher, Wendy Cannon, Siva R. Wigneshweraraj, Patricia Bordes, Martin Buck
Publikováno v:
Molecular Microbiology. 45:895-903
Transcriptional activator proteins that act upon the sigma54-containing form of the bacterial RNA polymerase belong to the extensive AAA+ superfamily of ATPases, members of which are found in all three kingdoms of life and function in diverse cellula
Publikováno v:
Nucleic Acids Research. 30:1016-1028
Protein footprints of the enhancer-dependent sigma54 protein, upon binding the Escherichia coli RNA polymerase core enzyme or upon forming closed promoter complexes, identified surface-exposed residues in sigma54 of potential functional importance at
Publikováno v:
Nucleic Acids Research. 29:1163-1174
In vitro DNA-binding and transcription properties of σ54 proteins with the invariant Arg383 in the putative helix–turn–helix motif of the DNA-binding domain substituted by lysine or alanine are described. We show that R383 contributes to maintai