A conserved insertion in protein-primed DNA polymerases is involved in primer terminus stabilisation. (Q38351607)

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6 November 2019

title

A conserved insertion in protein-primed DNA polymerases is involved in primer terminus stabilisation (English)

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6 November 2019

4

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6 November 2019

5

Margarita Salas

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6 November 2019

Emmanuelle Dufour

1

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6 November 2019

Irene Rodríguez

series ordinal

2

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6 November 2019

José M Lázaro

series ordinal

3

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6 November 2019

language of work or name

English

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publication date

1 August 2003

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Journal of Molecular Biology

6 November 2019

published in

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6 November 2019

volume

331

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6 November 2019

issue

4

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6 November 2019

page(s)

781-794

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Mechanisms of initiation of linear DNA replication in prokaryotes.

6 November 2019

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

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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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Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69

7 January 2021

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Structure of the replicating complex of a pol alpha family DNA polymerase

7 January 2021

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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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Gel fidelity assay measuring nucleotide misinsertion, exonucleolytic proofreading, and lesion bypass efficiencies

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A novel kinetic analysis to calculate nucleotide affinity of proofreading DNA polymerases. Application to phi 29 DNA polymerase fidelity mutants

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

7 January 2021

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A positively charged residue of phi29 DNA polymerase, highly conserved in DNA polymerases from families A and B, is involved in binding the incoming nucleotide

7 January 2021

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A DNA binding motif coordinating synthesis and degradation in proofreading DNA polymerases.

7 January 2021

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

7 January 2021

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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

7 January 2021

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Processive proofreading and the spatial relationship between polymerase and exonuclease active sites of bacteriophage phi29 DNA polymerase.

7 January 2021

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7 January 2021

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ø29 DNA polymerase residue Lys383, invariant at motif B of DNA-dependent polymerases, is involved in dNTP binding.

7 January 2021

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7 January 2021

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7 January 2021

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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

7 January 2021

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

7 January 2021

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7 January 2021

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7 January 2021

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10.1016/S0022-2836(03)00788-5

7 January 2021

Identifiers

DOI

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6 November 2019

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