The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition - Test2 - elhamkhani - TriplyDB

The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition

The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition

http://www.wikidata.org/entity/Q24542010

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PH1: an archaeovirus of Haloarcula hispanica related to SH1 and HHIV-2 Hepatitis B virus replication Involvement of the TPR2 subdomain movement in the activities of phi29 DNA polymerase Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases.Involvement of phage phi29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication DNA-Binding Proteins Essential for Protein-Primed Bacteriophage Φ29 DNA Replication Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage 29 tail The structure of a transcribing T7 RNA polymerase in transition from initiation to elongation.Bacteriophage protein-protein interactions Visualizing polynucleotide polymerase machines at work Deletion mutants of VPg reveal new cytopathology determinants in a picornavirus.Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid.Novel Podoviridae family bacteriophage infecting Weissella cibaria isolated from Kimchi.Functional eukaryotic nuclear localization signals are widespread in terminal proteins of bacteriophages The essential role of the 3' terminal template base in the first steps of protein-primed DNA replication Dual role of φ29 DNA polymerase Lys529 in stabilisation of the DNA priming-terminus and the terminal protein-priming residue at the polymerisation site Dissecting the role of the ϕ29 terminal protein DNA binding residues in viral DNA replication.Telomere-associated proteins add deoxynucleotides to terminal proteins during replication of the telomeres of linear chromosomes and plasmids in Streptomyces.Engineering Permissive Insertion Sites in the Bacteriophage Phi29 DNA-Linked Terminal Protein.Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity.My life with bacteriophage phi29.Protein-primed terminal transferase activity of hepatitis B virus polymerase.Multiple functions of DNA polymerases.Characterization of Interstrand DNA-DNA Cross-Links Derived from Abasic Sites Using Bacteriophage ϕ29 DNA Polymerase.Structural ensemble and dynamics of toroidal-like DNA shapes in bacteriophage ϕ29 exit cavity.Phage phi29 and Nf terminal protein-priming domain specifies the internal template nucleotide to initiate DNA replication Self-guanylylation of birnavirus VP1 does not require an intact polymerase activity site.Viral polymerases.Arrest of rolling circle amplification by protein-binding DNA aptamers.Synthetic biology approaches to biological containment: pre-emptively tackling potential risks.Structural changes of bacteriophage phi29 upon DNA packaging and release.Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity.Insights into the Determination of the Templating Nucleotide at the Initiation of φ29 DNA Replication.DNA packaging motor assembly intermediate of bacteriophage phi29.Improved artificial origins for phage Φ29 terminal protein-primed replication. Insights into early replication events.A Tyr residue in the reverse transcriptase domain can mimic the protein-priming Tyr residue in the terminal protein domain of a hepadnavirus P protein Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system.Involvement of residues of the 29 terminal protein intermediate and priming domains in the formation of a stable and functional heterodimer with the replicative DNA polymerase.Insights into new bacteriophages of Lactococcus garvieae belonging to the family Podoviridae.New insights in the ϕ29 terminal protein DNA-binding and host nucleoid localization functions.

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The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition

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The phi29 DNA polymerase:prote ...... ation to elongation transition

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The phi29 DNA polymerase:prote ...... ation to elongation transition

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The EMBO Journal

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The phi29 DNA polymerase:prote ...... ation to elongation transition

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Andrea J Berman

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Jimin Wang

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José M Lázaro

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Luis Blanco

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Miguel de Vega

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Satwik Kamtekar

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Thomas A Steitz

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A specific subdomain in phi29 DNA polymerase confers both processivity and strand-displacement capacity.

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase

Structural basis for initiation of transcription from an RNA polymerase-promoter complex

Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site

Structure of a transcribing T7 RNA polymerase initiation complex

Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70

Structure of the bacteriophage phi29 DNA packaging motor

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232800393

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protein structure

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