A5015730347- Bacteriophages and microbial interactions
- Genomics and Phylogenetic Studies
- Metabolism, Diabetes, and Cancer
- Pancreatic function and diabetes
- Cancer, Hypoxia, and Metabolism
- Diet, Metabolism, and Disease
- Bacterial Genetics and Biotechnology
- RNA and protein synthesis mechanisms
- Glycosylation and Glycoproteins Research
- Enzyme Structure and Function
- Plant Virus Research Studies
- Cancer Research and Treatments
- RNA modifications and cancer
- Pneumonia and Respiratory Infections
- Cellular transport and secretion
- Metabolism and Genetic Disorders
- Protein Structure and Dynamics
- Microbial Metabolic Engineering and Bioproduction
- Cytomegalovirus and herpesvirus research
- Viral Infections and Immunology Research
- Biochemical and Molecular Research
- Protein Kinase Regulation and GTPase Signaling
- Viral gastroenteritis research and epidemiology
- Antibiotics Pharmacokinetics and Efficacy
- Herpesvirus Infections and Treatments
Centre National de la Recherche Scientifique
1994-2024
Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2018-2024
Institut de Biologie Intégrative de la Cellule
2018-2024
CEA Paris-Saclay
2018-2024
Université Paris-Saclay
2018-2024
Laboratoire de Virologie Moléculaire et Structurale
2003-2021
Proteome Sciences (United Kingdom)
2007-2008
Laboratoire d'Enzymologie et Biochimie Structurales
1992-1997
A soluble flavoprotein that reoxidizes NADH and reduces molecular oxygen to water was purified from the facultative anaerobic human pathogen Streptococcus pneumoniae . The nucleotide sequence of nox , gene which encodes it, has been determined characterized at functional physiological level. Several mutants were obtained by insertion, nonsense or missense mutation. In extracts these strains, no oxidase activity could be measured, suggesting a single enzyme encoded having C44 in its active...
Siphophage SPP1 infects the gram-positive bacterium Bacillus subtilis using its long non-contractile tail and tail-tip. Electron microscopy (EM) previously allowed a low resolution assignment of most orf products belonging to these regions. We report here structure distal protein (Dit, gp19.1). The combination x-ray crystallography, EM, light scattering established that Dit is back-to-back dimer hexamers. However, fitting in virion EM maps was only possible with hexamer located between...
Summary Bacteriophages recognize and bind specific receptors to infect suitable hosts. Bacteriophage SPP1 targets at least two of the Bacillus subtilis cell envelope, glucosylated wall teichoic acids membrane protein YueB. Here, we identify a key virion for YueB binding trigger DNA ejection. Extracts from B. ‐infected cells applied affinity matrix led preferential capturing gp21 SPP1. To assess significance this interaction, isolated mutant phages specifically affected in binding. The...
The SPP1 siphophage uses its long non-contractile tail and tip to recognize infect the Gram-positive bacterium Bacillus subtilis. tail-end cap attached are critical components for host recognition opening of tube genome exit. In present work, we determined cryo-electron microscopic (cryo-EM) structure a complex formed by protein gp19.1 (Dit) N terminus downstream in genome, gp21(1-552) (Tal). This assembles two back-to-back stacked ring hexamers, interacting loosely, trimers with at both...
The majority of bacteriophages have a long non-contractile tail (Siphoviridae) that serves as conduit for viral DNA traffic from the phage capsid to host cell at beginning infection. 160-nm-long tube Bacillus subtilis bacteriophage SPP1 is shown be composed two major proteins (MTPs), gp17.1 and gp17.1*, ratio about 3:1. They share common amino-terminus, but latter species has approximately 10 kDa more than gp17.1. A CCC.UAA sequence with overlapping proline codons 3' end gene 17.1 drives...
Abstract Infection of bacteria by phages is a complex multi-step process that includes specific recognition the host cell, creation temporary breach in envelope, and ejection viral DNA into bacterial cytoplasm. These steps must be perfectly regulated to ensure efficient infection. Here we report dual function tail completion protein gp16.1 bacteriophage SPP1. First, has an auxiliary role assembly interface binds capsid connector. Second, necessary correct routing phage Viral particles...
Summary Bacteriophage SPP 1 is a nanomachine built to infect the bacterium B acillus subtilis . The phage particle composed of an icosahedric capsid, which contains viral DNA , and long non‐contractile tail. Capsids tails are produced in infected cells by two distinct morphogenetic pathways. Characterization suppressor‐sensitive mutant sus82 showed that it produces ‐filled capsids but unable assemble complete virions. Its purified have normal length lack narrow ring tapers tail end found at...
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Bacillus subtilis bacteriophage SPP1 is a lytic siphovirus first described 50 years ago. Its complete DNA sequence was reported in 1997. Here we present an updated annotation of the 44,016 bp genome and its correlation to different steps viral multiplication process. Five early polycistronic transcriptional units encode phage replication proteins lysis functions together with less characterized, mostly non-essential, functions. Late transcription drives synthesis necessary for particles...
During the reaction catalyzed by phosphofructokinase (EC 2.7.1.11) from Escherichia coli, phosphoryl group transferred ATP interacts with Thr-125 [Shirakihara, Y. & Evans, P. R. (1988) J. Mol. Biol. 204, 973-994]. The replacement of serine changes saturation fructose 6-phosphate cooperative to hyperbolic and abolishes allosteric inhibition phosphoenolpyruvate. same changes, a that is no longer an activity inhibited phosphoenolpyruvate, are observed wild-type when adenosine...
Abstract The kinetics of the reverse reaction catalyzed by Escherichia coli phosphofructokinase, i.e., synthesis ATP and fructose‐6‐phosphate from ADP fructose‐1,6‐bisphosphate, have been studied at different pH values, 6 to 9.2. Hyperbolic saturations enzyme are observed for both substrates. affinity fructose‐1,6‐bisphosphate decreases with following ionization a group pK 6.6, whereas catalytic rate constant perhaps controlled 6. Several arguments show that 6.6 is probably carboxyl Asp 127,...
The pH dependence of the enzymic properties phosphofructokinase from Escherichia coli was compared to those two mutants in which one carboxyl group active site has been removed either Asp127 or Asp129. All measurements activity were made presence allosteric activator ADP GDP eliminate any cooperative process. Asp129 is a crucial residue for since its conversion Ser decreases catalytic by 2—3 orders magnitude both forward and reverse reactions, but ionization not directly related activity....
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTTetramer-Dimer Equilibrium of Phosphofructokinase and Formation Hybrid TetramersGisele Le Bras, Isabelle Auzat, Jean-Renaud GarelCite this: Biochemistry 1995, 34, 40, 13203–13210Publication Date (Print):October 10, 1995Publication History Published online1 May 2002Published inissue 10 October 1995https://pubs.acs.org/doi/10.1021/bi00040a036https://doi.org/10.1021/bi00040a036research-articleACS PublicationsRequest reuse permissionsArticle...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRole of Residue 161 in the Allosteric Transitions Two Bacterial PhosphofructokinasesIsabelle Auzat, W. Malcolm Byrnes, Jean-Renaud Garel, and Simon H. ChangCite this: Biochemistry 1995, 34, 21, 7062–7068Publication Date (Print):May 30, 1995Publication History Published online1 May 2002Published inissue 30 1995https://pubs.acs.org/doi/10.1021/bi00021a018https://doi.org/10.1021/bi00021a018research-articleACS PublicationsRequest reuse...
With the analog adenosine-5'-0-(3-thiotriphosphate) (A TP-γS) instead of ATP as a substrate, catalytic rate-constant k cat allosteric phosphofructokinase from Escherichia coli becomes independent pH between 6 and 9 following ionization group pK=7. This marked change in pH-dependence t could be due to lower pK y-thiophosphate ATP-γS compared that they-phosphate or rate-limiting step.