Plasmid replication initiator protein RepD increases the processivity of PcrA DNA helicase. 1999

P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK andSchool of Biochemistry and Molecular Biology, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, UK.

The replication initiator protein RepD encoded by the Staphylococcus chloramphenicol resistance plasmid pC221 stimulates the helicase activity of the Bacillus stearothermophilus PcrA DNA helicase in vitro. This stimulatory effect seems to be specific for PcrA and differs from the stimulatory effect of the Escherichia coli ribosomal protein L3. Whereas L3 stimulates the PcrA helicase activity by promoting co-operative PcrA binding onto its DNA substrate, RepD stimulates the PcrA helicase activity by increasing the processivity of the enzyme and enables PcrA to displace DNA from a nicked substrate. The implication of these results is that PcrA is the helicase recruited into the replisome by RepD during rolling circle replication of plasmids of the pT181 family.

UI MeSH Term Description Entries
D008957 Models, Genetic Theoretical representations that simulate the behavior or activity of genetic processes or phenomena. They include the use of mathematical equations, computers, and other electronic equipment. Genetic Models,Genetic Model,Model, Genetic
D010957 Plasmids Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS. Episomes,Episome,Plasmid
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002702 Chloramphenicol Resistance Nonsusceptibility of bacteria to the action of CHLORAMPHENICOL, a potent inhibitor of protein synthesis in the 50S ribosomal subunit where amino acids are added to nascent bacterial polypeptides. Chloramphenicol Resistances
D004261 DNA Replication The process by which a DNA molecule is duplicated. Autonomous Replication,Replication, Autonomous,Autonomous Replications,DNA Replications,Replication, DNA,Replications, Autonomous,Replications, DNA
D004265 DNA Helicases Proteins that catalyze the unwinding of duplex DNA during replication by binding cooperatively to single-stranded regions of DNA or to short regions of duplex DNA that are undergoing transient opening. In addition, DNA helicases are DNA-dependent ATPases that harness the free energy of ATP hydrolysis to translocate DNA strands. ATP-Dependent DNA Helicase,DNA Helicase,DNA Unwinding Protein,DNA Unwinding Proteins,ATP-Dependent DNA Helicases,DNA Helicase A,DNA Helicase E,DNA Helicase II,DNA Helicase III,ATP Dependent DNA Helicase,ATP Dependent DNA Helicases,DNA Helicase, ATP-Dependent,DNA Helicases, ATP-Dependent,Helicase, ATP-Dependent DNA,Helicase, DNA,Helicases, ATP-Dependent DNA,Helicases, DNA,Protein, DNA Unwinding,Unwinding Protein, DNA,Unwinding Proteins, DNA
D004268 DNA-Binding Proteins Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins
D000251 Adenosine Triphosphatases A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D001411 Geobacillus stearothermophilus A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products. Bacillus stearothermophilus,Bacillus thermoliquefaciens
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial

Related Publications

P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
May 2013, Nucleic acids research,
P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
July 2009, Biochemistry,
P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
April 2010, Nucleic acids research,
P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
May 2002, Molecular genetics and genomics : MGG,
P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
August 1995, Biochemical Society transactions,
P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
June 2015, PLoS genetics,
P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
May 1996, Proceedings of the National Academy of Sciences of the United States of America,
P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
November 2002, The Journal of biological chemistry,
P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
July 1996, The Journal of biological chemistry,
P Soultanas, and M S Dillingham, and F Papadopoulos, and S E Phillips, and C D Thomas, and D B Wigley
November 1993, Science (New York, N.Y.),
Copied contents to your clipboard!