phi29 DNA polymerase residue Phe128 of the highly conserved (S/T)Lx(2)h motif is required for a stable and functional interaction with the terminal protein (Q34163492)

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English	phi29 DNA polymerase residue Phe128 of the highly conserved (S/T)Lx(2)h motif is required for a stable and functional interaction with the terminal protein	scientific article

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scholarly article

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PubMed publication ID

31 July 2017

phi29 DNA polymerase residue Phe128 of the highly conserved (S/T)Lx(2)h motif is required for a stable and functional interaction with the terminal protein (English)

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Europe PubMed Central

PubMed publication ID

31 July 2017

Margarita Salas

3

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Margarita Salas

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31 July 2017

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Irene Rodríguez

1

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31 July 2017

José M Lázaro

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31 July 2017

Miguel de Vega

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31 July 2017

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1 January 2003

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31 July 2017

Journal of Molecular Biology

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31 July 2017

325

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31 July 2017

1

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31 July 2017

85-97

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Europe PubMed Central

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31 July 2017

Protein-priming of DNA replication

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Characterization and purification of a phage phi 29-encoded DNA polymerase required for the initiation of replication

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Initiation of phi 29 DNA replication occurs at the second 3' nucleotide of the linear template: a sliding-back mechanism for protein-primed DNA replication.

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In vitro protein-primed initiation of pneumococcal phage Cp-1 DNA replication occurs at the third 3' nucleotide of the linear template: a stepwise sliding-back mechanism

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Protein-primed DNA replication: a transition between two modes of priming by a unique DNA polymerase

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Relating structure to function in phi29 DNA polymerase

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Role of the "YxGG/A" motif of Phi29 DNA polymerase in protein-primed replication

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An aspartic acid residue in TPR-1, a specific region of protein-priming DNA polymerases, is required for the functional interaction with primer terminal protein

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Phi 29 DNA polymerase requires the N-terminal domain to bind terminal protein and DNA primer substrates

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phi29 DNA polymerase residue Ser122, a single-stranded DNA ligand for 3'-5' exonucleolysis, is required to interact with the terminal protein

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Phi29 DNA polymerase residues Tyr59, His61 and Phe69 of the highly conserved ExoII motif are essential for interaction with the terminal protein

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Structure-function analysis of 3'-->5'-exonuclease of DNA polymerases

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Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins

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Purification of bacteriophage phi 29 DNA polymerase

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Helix-destabilizing activity of phi 29 single-stranded DNA binding protein: effect on the elongation rate during strand displacement DNA replication.

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A conserved 3'----5' exonuclease active site in prokaryotic and eukaryotic DNA polymerases

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An invariant lysine residue is involved in catalysis at the 3'-5' exonuclease active site of eukaryotic-type DNA polymerases

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Phage phi 29 DNA polymerase residues involved in the proper stabilisation of the primer-terminus at the 3'-5' exonuclease active site

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The putative coiled coil domain of the phi 29 terminal protein is a major determinant involved in recognition of the origin of replication

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Sequence requirements for protein-primed initiation and elongation of phage O29 DNA replication

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Crystal structure of Thermus aquaticus DNA polymerase

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Crystal Structure of a pol α Family Replication DNA Polymerase from Bacteriophage RB69

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Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius

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Crystal structure of DNA polymerase from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1

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Crystal structure of an archaebacterial DNA polymerase

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Effects of internal deletions on the priming activity of the phage phi 29 terminal protein

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Characterization of the phage phi 29 protein p5 as a single-stranded DNA binding protein. Function in phi 29 DNA-protein p3 replication

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Physical map of bacteriophage phi29 DNA.

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Initiation of phage phi 29 DNA replication in vitro: formation of a covalent complex between the terminal protein, p3, and 5'-dAMP.

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Identifiers

10.1016/S0022-2836(02)01130-0

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

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