scholarly journals Utility of the Bacteriophage RB69 Polymerase gp43 as a Surrogate Enzyme for Herpesvirus Orthologs

Viruses ◽  
2013 ◽  
Vol 5 (1) ◽  
pp. 54-86 ◽  
Author(s):  
Nicholas Bennett ◽  
Matthias Götte
Keyword(s):  
Bacteriophage Rb69

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

Cell ◽  
1997 ◽  
Vol 89 (7) ◽  
pp. 1087-1099 ◽  
Author(s):  
J. Wang ◽  
A.K.M.A. Sattar ◽  
C.C. Wang ◽  
J.D. Karam ◽  
W.H. Konigsberg ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dna Polymerase ◽  
Bacteriophage Rb69

scholarly journals Protein Determinants of RNA Binding by DNA Polymerase of the T4-related Bacteriophage RB69

2002 ◽  
Vol 277 (36) ◽  
pp. 33041-33048 ◽  
Author(s):  
Vasiliy M. Petrov ◽  
San-san Ng ◽  
Jim D. Karam
Keyword(s):  
Dna Polymerase ◽  
Rna Binding ◽  
Bacteriophage Rb69

scholarly journals Interacting Fidelity Defects in the Replicative DNA Polymerase of Bacteriophage RB69

2000 ◽  
Vol 276 (13) ◽  
pp. 10387-10397 ◽  
Author(s):  
Anna Bebenek ◽  
Holly Kloos Dressman ◽  
Geraldine T. Carver ◽  
San-san Ng ◽  
Vasiliy Petrov ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Bacteriophage Rb69

A New Look at Old Mutants of T4 DNA Polymerase

Genetics ◽  
1998 ◽  
Vol 148 (4) ◽  
pp. 1535-1538
Author(s):  
Nancy G Nossal
Keyword(s):  
Crystal Structure ◽  
Dna Polymerase ◽  
Bacteriophage T4 ◽  
Polymerase Mutants ◽  
Bacteriophage Rb69 ◽  
New Look

Abstract The DNA polymerase and nuclease activities of bacteriophage T4 DNA polymerase mutants are discussed in the context of the crystal structure of the closely related bacteriophage RB69 DNA polymerase.

scholarly journals Kinetics of Mismatch Formation opposite Lesions by the Replicative DNA Polymerase from Bacteriophage RB69

Biochemistry ◽  
2010 ◽  
Vol 49 (11) ◽  
pp. 2317-2325 ◽  
Author(s):  
Matthew Hogg ◽  
Jean Rudnicki ◽  
John Midkiff ◽  
Linda Reha-Krantz ◽  
Sylvie Doublié ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Bacteriophage Rb69 ◽  
Kinetics Of

scholarly journals Dissecting the Fidelity of Bacteriophage RB69 DNA Polymerase: Site-Specific Modulation of Fidelity by Polymerase Accessory Proteins

Genetics ◽  
2002 ◽  
Vol 162 (3) ◽  
pp. 1003-1018 ◽  
Author(s):  
Anna Bebenek ◽  
Geraldine T Carver ◽  
Holly Kloos Dressman ◽  
Farid A Kadyrov ◽  
Joseph K Haseman ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Important Determinant ◽  
Mutation Rates ◽  
Accessory Proteins ◽  
Wild Type ◽  
Mutational Spectra ◽  
Base Selection ◽  
Bacteriophage Rb69

Abstract Bacteriophage RB69 encodes a replicative B-family DNA polymerase (RB69 gp43) with an associated proofreading 3′ exonuclease. Crystal structures have been determined for this enzyme with and without DNA substrates. We previously described the mutation rates and kinds of mutations produced in vivo by the wild-type (Pol+ Exo+) enzyme, an exonuclease-deficient mutator variant (Pol+ Exo-), mutator variants with substitutions at Tyr567 in the polymerase active site (PolM Exo+), and the double mutator PolM Exo-. Comparing the mutational spectra of the Pol+ Exo- and Pol+ Exo+ enzymes revealed the patterns and efficiencies of proofreading, while Tyr567 was identified as an important determinant of base-selection fidelity. Here, we sought to determine how well the fidelities of the same enzymes are reflected in vitro. Compared to their behavior in vivo, the three mutator polymerases exhibited modestly higher mutation rates in vitro and their mutational predilections were also somewhat different. Although the RB69 gp43 accessory proteins exerted little or no effect on total mutation rates in vitro, they strongly affected mutation rates at many specific sites, increasing some rates and decreasing others.

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