A broad host range replicon with different requirements for replication initiation in three bacterial species
暂无分享,去创建一个
D. Helinski | R. Caspi | I. Konieczny | D R Helinski | R Caspi | M Pacek | I Konieczny | G Consiglieri | A Toukdarian | Donald R. Helinski | Ron Caspi | Marcin Pacek | Giac Consiglieri | Aresa Toukdarian | Marcin Pacek
[1] D. Bastia,et al. The replication initiator protein pi of the plasmid R6K specifically interacts with the host-encoded helicase DnaB. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[2] R. Lurz,et al. Complexes at the replication origin of Bacillus subtilis with homologous and heterologous DnaA protein. , 1997, Journal of molecular biology.
[3] W. Messer,et al. The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli , 2000, Molecular microbiology.
[4] D. Bastia,et al. Mechanistic studies of initiator–initiator interaction and replication initiation , 1998, The EMBO journal.
[5] N. Dixon,et al. Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectroscopy. , 1997, Biochemical and biophysical research communications.
[6] S. Biswas,et al. Mechanism of DNA binding by the DnaB helicase of Escherichia coli: analysis of the roles of domain gamma in DNA binding. , 1999, Biochemistry.
[7] D. Bastia,et al. Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[8] Tania A Baker,et al. Polymerases and the Replisome: Machines within Machines , 1998, Cell.
[9] E. Lanka,et al. The dnaC protein of Escherichia coli. Purification, physical properties and interaction with dnaB protein. , 1983, Nucleic acids research.
[10] D. Helinski,et al. Interactions of DnaA Proteins from Distantly Related Bacteria with the Replication Origin of the Broad Host Range Plasmid RK2* , 2000, The Journal of Biological Chemistry.
[11] B. Holloway,et al. Control of Pyrimidine Biosynthesis in Pseudomonas aeruginosa , 1968, Journal of bacteriology.
[12] J. Pogliano,et al. SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF , 1995, Cell.
[13] D. Helinski,et al. The Plasmid RK2 Initiation Protein Binds to the Origin of Replication as a Monomer (*) , 1996, The Journal of Biological Chemistry.
[14] A. West,et al. Proteins encoded by the trans-acting replication and maintenance regions of broad host range plasmid RK2. , 1984, Plasmid.
[15] Edward H. Egelman,et al. The hexameric E. coli DnaB helicase can exist in different Quaternary states. , 1996, Journal of molecular biology.
[16] J. Drake,et al. Molecular Biology of Bacteriophage T4 , 1994 .
[17] Christopher M Thomas,et al. Analysis of the trfA region of broad host-range plasmid RK2 by transposon mutagenesis and identification of polypeptide products. , 1984, Journal of molecular biology.
[18] D. Helinski,et al. Interactions of plasmid-encoded replication initiation proteins with the origin of DNA replication in the broad host range plasmid RK2. , 1991, The Journal of biological chemistry.
[19] S. Biswas,et al. Structure and function of Escherichia coli DnaB protein: role of the N-terminal domain in helicase activity. , 1994, Biochemistry.
[20] D. Belin,et al. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter , 1995, Journal of bacteriology.
[21] Christopher M. Thomas. Promiscuous plasmids of gram-negative bacteria , 1989 .
[22] H. Echols,et al. Specialized nucleoprotein structures at the origin of replication of bacteriophage lambda: complexes with lambda O protein and with lambda O, lambda P, and Escherichia coli DnaB proteins. , 1985, Proceedings of the National Academy of Sciences of the United States of America.
[23] T. Steitz,et al. DnaB from Thermus aquaticus Unwinds Forked Duplex DNA with an Asymmetric Tail Length Dependence* , 1999, The Journal of Biological Chemistry.
[24] D. Helinski,et al. Helicase Delivery and Activation by DnaA and TrfA Proteins during the Initiation of Replication of the Broad Host Range Plasmid RK2* , 1997, The Journal of Biological Chemistry.
[25] F. Fang,et al. Broad-host-range properties of plasmid RK2: importance of overlapping genes encoding the plasmid replication initiation protein TrfA , 1991, Journal of bacteriology.
[26] J M Carazo,et al. A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. , 1995, Journal of structural biology.
[27] A. Kornberg,et al. The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties. , 1989, The Journal of biological chemistry.
[28] J. Thompson,et al. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. , 1997, Nucleic acids research.
[29] E. Egelman. Bacterial helicases. , 1998, Journal of structural biology.
[30] D. Saluja,et al. Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252, dnaB70, dnaB43, and dnaB454 , 1995, Journal of bacteriology.
[31] T. Baker,et al. Extensive unwinding of the plasmid template during staged enzymatic initiation of DNA replication from the origin of the Escherichia coli chromosome , 1986, Cell.
[32] J. Hurwitz,et al. Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro. , 1975, Proceedings of the National Academy of Sciences of the United States of America.
[33] D. Helinski,et al. Role of TrfA and DnaA Proteins in Origin Opening during Initiation of DNA Replication of the Broad Host Range Plasmid RK2* , 1997, The Journal of Biological Chemistry.
[34] Detlef D. Leipe,et al. The bacterial replicative helicase DnaB evolved from a RecA duplication. , 2000, Genome research.
[35] S. Um,et al. Cryptic single-stranded-DNA binding activities of the phage lambda P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNA. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[36] D. Helinski,et al. Copy-up mutants of the plasmid RK2 replication initiation protein are defective in coupling RK2 replication origins. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[37] D. Helinski,et al. The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[38] T. Baker,et al. In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome. , 1987, The Journal of biological chemistry.
[39] S. Moriya,et al. Subcellular localization of Dna‐initiation proteins of Bacillus subtilis: evidence that chromosome replication begins at either edge of the nucleoids , 2000, Molecular microbiology.
[40] K. Marians,et al. Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. , 1994, The Journal of biological chemistry.
[41] Thomas L. Madden,et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. , 1997, Nucleic acids research.
[42] C. McHenry,et al. Coupling of a Replicative Polymerase and Helicase: A τ–DnaB Interaction Mediates Rapid Replication Fork Movement , 1996, Cell.
[43] R. Sclafani,et al. Deoxyribonucleic acid initiation mutation dnaB252 is suppressed by elevated dnaC+ gene dosage , 1981, Journal of bacteriology.
[44] A. Kornberg,et al. Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome , 1988, Cell.
[45] J. Marszalek,et al. DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli. , 1994, The Journal of biological chemistry.
[46] M. Vicente,et al. Cloning vectors, derived from a naturally occurring plasmid of Pseudomonas savastanoi, specifically tailored for genetic manipulations in Pseudomonas. , 1990, Gene.
[47] A. Kornberg,et al. Fine balance in the regulation of DnaB helicase by DnaC protein in replication in Escherichia coli. , 1991, The Journal of biological chemistry.
[48] D. Helinski,et al. Replication of derivatives of the broad host range plasmid RK2 in two distantly related bacteria. , 1983, Plasmid.
[49] I. Konieczny,et al. The Requirement for Molecular Chaperones in λDNA Replication Is Reduced by the Mutation π in λP Gene, Which Weakens the Interaction between λP Protein and DnaB Helicase (*) , 1995, The Journal of Biological Chemistry.
[50] J. Lebowitz,et al. The Escherichia coli dnaB replication protein is a DNA helicase. , 1986, The Journal of biological chemistry.
[51] D. Bastia,et al. Mechanism of recruitment of DnaB helicase to the replication origin of the plasmid pSC101. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[52] D. Helinski,et al. Replication Origin of the Broad Host Range Plasmid RK2 , 1998, The Journal of Biological Chemistry.
[53] Detlef D. Leipe,et al. Did DNA replication evolve twice independently? , 1999, Nucleic acids research.
[54] M. Pacek,et al. DnaA Box Sequences as the Site for Helicase Delivery during Plasmid RK2 Replication Initiation in Escherichia coli * , 2001, Journal of Biological Chemistry.
[55] D. Helinski,et al. The sequence encoding the 43-kilodalton trfA protein is required for efficient replication or maintenance of minimal RK2 replicons in Pseudomonas aeruginosa. , 1987, Plasmid.