Affiliation: Imperial College
- Sensor I threonine of the AAA+ ATPase transcriptional activator PspF is involved in coupling nucleotide triphosphate hydrolysis to the restructuring of sigma 54-RNA polymeraseJorg Schumacher
Division of Biology, Imperial College London, London SW7 2AZ, UK
J Biol Chem 282:9825-33. 2007..We propose that hydrolysis is relayed via Thr(148) to loop 2 creating motions that provide mechanical force to the GAFTGA loop 1 that contacts sigma(54)...
- Structures and organisation of AAA+ enhancer binding proteins in transcriptional activationJorg Schumacher
Division of Biology, Imperial College London, London, SW7 2AZ, UK
J Struct Biol 156:190-9. 2006..Parallels with the substrate binding elements near the central pore of other AAA+ members are drawn. We propose a structural model of EBPs in complex with a sigma(54)-RNAP-promoter complex...
- Mechanism of homotropic control to coordinate hydrolysis in a hexameric AAA+ ring ATPaseJorg Schumacher
Division of Biology, Imperial College London, London SW7 2AZ, UK
J Mol Biol 381:1-12. 2008..Homotropic coordination is functionally important to remodel the sigma(54) promoter. We propose a structural symmetry-based model for homotropic control in the AAA(+) characteristic ring architecture...
- The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: identifying a surface that binds sigma 54Patricia Bordes
Department of Biological Sciences, Sir Alexander Fleming Building, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom
Proc Natl Acad Sci U S A 100:2278-83. 2003....
- Structural insights into the activity of enhancer-binding proteinsMathieu Rappas
Department of Biological Sciences, Imperial College London, London, SW7 2AZ, UK
Science 307:1972-5. 2005..Comparing enhancer-binding structures in different nucleotide states and mutational analysis led us to propose nucleotide-dependent conformational changes that free the loops for association with sigma54...
- Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspFMathieu Rappas
Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK
J Mol Biol 357:481-92. 2006..Striking similarities in nucleotide-specific conformational changes and atomic switch exist between PspF and the large T antigen helicase, suggesting conservation in the origin of those events amongst AAA(+) proteins...
- ATP-dependent transcriptional activation by bacterial PspF AAA+proteinJorg Schumacher
Department of Biological Sciences, Sir Alexander Fleming Building, Imperial College London, South Kensington Campus, London SW7 2AZ, UK
J Mol Biol 338:863-75. 2004..Substitution of this arginine residue results in nucleotide-independent formation of hexameric rings, structurally linking the putative R-finger and, by inference, a specific nucleotide interaction to the control of PspF oligomerisation...
- Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activatorNicolas Joly
Division of Biology, Sir Alexander Fleming Building, Imperial College London, London SW7 2AZ, United Kingdom
J Biol Chem 281:34997-5007. 2006..Esigma54 complex provides clear biochemical evidence for heterogeneous nucleotide occupancy in this AAA+ protein. Based on our data, we propose a stochastic nucleotide binding and a coordinated hydrolysis mechanism in PspF1-275 hexamers...
- Dissecting the ATP hydrolysis pathway of bacterial enhancer-binding proteinsDaniel Bose
Division of Molecular Bioscience, Faculty of Natural Sciences, Imperial College London, South Kensington, London, SW7 2AZ, U K
Biochem Soc Trans 36:83-8. 2008..In the present article, we review some of the key nucleotides, mutations and techniques used and how they have contributed towards our understanding of the function of bEBPs...
- Functional roles of the pre-sensor I insertion sequence in an AAA+ bacterial enhancer binding proteinPatricia C Burrows
Department of Life Sciences, Division of Biology, Imperial College London, London, UK
Mol Microbiol 73:519-33. 2009....
- Modus operandi of the bacterial RNA polymerase containing the sigma54 promoter-specificity factorSivaramesh Wigneshweraraj
Department of Microbiology, Division of Investigative Sciences, Faculty of Medicine and Centre for Molecular Microbiology and Infection, Imperial College London, SW7 2AZ, UK
Mol Microbiol 68:538-46. 2008..Here, we summarize our current understanding of the interactions the sigma(54) factor makes with the bacterial transcription machinery...
- Visualizing the organization and reorganization of transcription complexes for gene expressionPatricia C Burrows
Division of Molecular Biosciences, Department of Life Sciences, Imperial College London, London, UK
Biochem Soc Trans 36:776-9. 2008....
- Regulation of the co-evolved HrpR and HrpS AAA+ proteins required for Pseudomonas syringae pathogenicityMilija Jovanovic
Division of Biology, Faculty of Natural Sciences, Sir Alexander Fleming Building, Imperial College London, London SW7 2AZ, UK
Nat Commun 2:177. 2011..The distinct HrpR and HrpS functionalities suggest how partial paralogue degeneration has potentially led to a novel control mechanism for EBPs and indicate subunit-specific roles for EBPs in σ(54)-RNA polymerase activation...
- Mechanism of action of the Escherichia coli phage shock protein PspA in repression of the AAA family transcription factor PspFSarah Elderkin
Department of Biological Sciences, Imperial College of Science Technology and Medicine, Biomedical Sciences Building, Imperial College Road, London SW7 2AZ, UK
J Mol Biol 320:23-37. 2002....
- Nitrogen and carbon status are integrated at the transcriptional level by the nitrogen regulator NtrC in vivoJorg Schumacher
Division of Cell and Molecular Biology, Imperial College London, London, United Kingdom
MBio 4:e00881-13. 2013..We propose an in vivo model in which α-ketoglutarate can derepress nitrogen regulation despite nitrogen sufficiency...
- In vitro and in vivo methodologies for studying the Sigma 54-dependent transcriptionMartin Buck
Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW7 2AZ, UK
Methods Mol Biol 1276:53-79. 2015..We also present in vivo methodologies that are used to study the impact of physiological processes, metabolic states, global signalling networks, and cellular architecture on the control of σ(54)-dependent gene expression. ..
- Negative Autogenous Control of the Master Type III Secretion System Regulator HrpL in Pseudomonas syringaeChristopher Waite
Department of Life Sciences, Imperial College London, London, United Kingdom
MBio 8:. 2017..We argue that negative feedback on HrpL activity fine-tunes expression of the T3SS regulon to minimize the elicitation of plant defenses...
- Interplay among Pseudomonas syringae HrpR, HrpS and HrpV proteins for regulation of the type III secretion systemMilija Jovanovic
Department of Life Sciences, Imperial College London, London, UK
FEMS Microbiol Lett 356:201-11. 2014..Deletion analysis of HrpR and HrpS proteins showed that C-terminal parts of HrpR and HrpS confer determinants indispensable for their self-assembly. ..
- Rewiring cell signalling through chimaeric regulatory protein engineeringBaojun Wang
Department of Mathematics, Imperial College London, London SW7 2AZ, U K
Biochem Soc Trans 41:1195-200. 2013..We envisage that engineered chimaeric regulatory proteins can play an important role to aid both forward and reverse engineering of biological systems for many desired applications. ..