A5019224218- Plant Virus Research Studies
- Protein Structure and Dynamics
- Plant-Microbe Interactions and Immunity
- Microbial Natural Products and Biosynthesis
- Bacterial Genetics and Biotechnology
- Microbial Metabolic Engineering and Bioproduction
- Immune Cell Function and Interaction
- ATP Synthase and ATPases Research
- Enzyme Structure and Function
- Adenosine and Purinergic Signaling
- Synthesis and Catalytic Reactions
- Amino Acid Enzymes and Metabolism
- Transgenic Plants and Applications
- Antimicrobial Peptides and Activities
- Photoreceptor and optogenetics research
- thermodynamics and calorimetric analyses
- Biochemical and Molecular Research
- Peptidase Inhibition and Analysis
- Ubiquitin and proteasome pathways
- Machine Learning in Bioinformatics
- Mass Spectrometry Techniques and Applications
- Monoclonal and Polyclonal Antibodies Research
- Porphyrin Metabolism and Disorders
- Metal-Catalyzed Oxygenation Mechanisms
- Corrosion Behavior and Inhibition
Durham University
2008-2021
Allostery in bacterial transcription factors arises from changes global low-frequency protein dynamics. Amino acids that regulate dynamics are identified and seen to be evolutionarily conserved.
Plant nucleotide-binding leucine-rich repeat (NLR) proteins enable cells to respond pathogen attack. Several NLRs act in the nucleus; however, conserved nuclear targets that support their role immunity are unknown. Previously, we noted a structural homology between domain of and DNA replication origin-binding Cdc6/Orc1 proteins. Here show NB-ARC (nucleotide-binding, Apaf-1, R-proteins, CED-4) Rx1 NLR potato binds nucleic acids. induces ATP-dependent bending melting vitro, dependent upon...
Allostery is a fundamental process by which ligand binding to protein alters its activity at distant site. Both experimental and theoretical evidence demonstrate that allostery can be communicated through altered slow relaxation dynamics without conformational change. The catabolite activator (CAP) of Escherichia coli an exemplar for the analysis such entropically driven allostery. Negative in CAP occurs between identical cAMP sites. Changes cAMP-binding pocket therefore impact allosteric...
Carbon dioxide is fundamental to the physiology of all organisms. There considerable interest in precise molecular mechanisms that organisms use directly sense CO(2). Here we demonstrate a mammalian recombinant G-protein-activated adenylyl cyclase and related Rv1625c Mycobacterium tuberculosis are specifically stimulated by Stimulation occurred at physiological concentrations CO(2) through increased k(cat). affinity enzyme for metal co-factor, but contact with was not necessary as interacted...
The cyclic AMP-dependent transcriptional regulator GlxR from Corynebacterium glutamicum is a member of the super-family CRP/FNR (cyclic AMP receptor protein/fumarate and nitrate reduction regulator) regulators that play central roles in bacterial metabolic regulatory networks. In C. glutamicum, which widely used for industrial production amino acids serves as non-pathogenic model organism members Corynebacteriales including Mycobacterium tuberculosis, homodimer controls transcription large...
Allostery is a fundamental process by which ligand binding to protein alters its activity at distant site. There considerable evidence that allosteric cooperativity can be communicated the modulation of dynamics without conformational change. The Catabolite Activator Protein (CAP) Escherichia coli an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis highlights role global low-frequency in allostery CAP and...
The intracellular immune receptor Rx1 of potato (Solanum tuberosum), which confers effector-triggered immunity to Potato virus X, consists a central nucleotide-binding domain (NB-ARC) flanked by carboxyl-terminal leucine-rich repeat (LRR) and an amino-terminal coiled-coil (CC) domain. activity is strictly regulated interdomain interactions between the NB-ARC LRR, but contribution CC in regulating or signaling not fully understood. Therefore, we used structure-informed approach investigate...
The identification of CO2-binding proteins is crucial to understanding CO2-regulated molecular processes. CO2 can form a reversible posttranslational modification through carbamylation neutral N-terminal α-amino or lysine ε-amino groups. We have previously developed triethyloxonium (TEO) ion as chemical proteomics tool for covalent trapping carbamates, and here, we deploy TEO identify ubiquitin mammalian protein. use 13C-NMR spectroscopy demonstrate that forms carbamates on the N terminus...
Plant nucleotide-binding leucine-rich repeat (NLR) proteins enable plants to recognize and respond pathogen attack. Previously, we demonstrated that the Rx1 NLR of potato is able bind bend DNA in vitro. binding situ requires its genuine activation following perception. However, it unknown whether other are also DNA. Nor known how relates ATPase activity intrinsic switch function required immune activation. Here investigate these issues using a recombinant protein corresponding N-terminal...
Plant NLR proteins enable the immune system to recognize and respond pathogen attack. An early consequence of activation is transcriptional reprogramming. Some NLRs have been shown act in nucleus interact with transcription factors. The Rx1 protein potato binds distorts double-stranded DNA. However, components chromatin-localized complex are largely unknown. Here, we report a physical functional interaction between NbDBCP, bromodomain-containing chromatin-interacting protein. NbDBCP...