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 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 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

scholarly journals An improved and readily available version of Bst DNA Polymerase for LAMP, and applications to COVID-19 diagnostics

2020 ◽  
Author(s):  
Andre Maranhao ◽  
Sanchita Bhadra ◽  
Inyup Paik ◽  
David Walker ◽  
Andrew D. Ellington
Keyword(s):  
Dna Polymerase ◽  
Bacillus Stearothermophilus ◽  
Rna Binding ◽  
Dna Polymerases ◽  
Point Mutations ◽  
Reverse Transcriptase Activity ◽  
Isothermal Amplification ◽  
Binding Domains ◽  
Great Utility ◽  
The Impact

AbstractDespite the fact that strand-displacing activity is of great utility for a variety of applications, including isothermal amplification assays, there are relatively few strand-displacing DNA polymerases. In particular, the thermotolerant DNA polymerase from Geobacillus stearothermophilus (previously Bacillus stearothermophilus), Bst DNA polymerase (Bst DNAP), is used in a variety of assays, including loop-mediated isothermal amplification. However, despite its wide use, its properties remain open to improvement, as has been demonstrated by a variety of engineering efforts, including the identification of point mutations that impact its robustness, strand-displacement capabilities, and nascent reverse transcriptase activity.Interestingly, a strategy that has been commonly used to alter the capabilities of DNA polymerases, the addition of additional DNA- or RNA-binding domains, has yet to be applied to Bst DNAP. To this end, we now show that by adding fusion domains the performance of Bst DNAP in isothermal amplification assays, including its nascent RT activity, can be greatly improved. The impact of these improvements on the development of LAMP assays for the detection of SARS-CoV-2 is fully explored.

scholarly journals Evolution of RNA-binding Specificity in T4 DNA Polymerase

1997 ◽  
Vol 272 (28) ◽  
pp. 17703-17710 ◽  
Author(s):  
Chien-Chia Wang ◽  
Andrey Pavlov ◽  
Jim D. Karam
Keyword(s):  
Dna Polymerase ◽  
Rna Binding ◽  
Binding Specificity

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 Efficient Translation of Epstein-Barr Virus (EBV) DNA Polymerase Contributes to the Enhanced Lytic Replication Phenotype of M81 EBV

2017 ◽  
Vol 92 (6) ◽  
Author(s):  
Trenton Mel Church ◽  
Dinesh Verma ◽  
Jacob Thompson ◽  
Sankar Swaminathan
Keyword(s):  
Nasopharyngeal Carcinoma ◽  
Dna Polymerase ◽  
Epstein Barr Virus ◽  
Rna Binding ◽  
Virus Production ◽  
Protein Translation ◽  
Lytic Replication ◽  
Barr Virus ◽  
Ebv Dna ◽  
Epstein Barr

ABSTRACTEpstein-Barr virus (EBV) is linked to the development of both lymphoid and epithelial malignancies worldwide. The M81 strain of EBV, isolated from a Chinese patient with nasopharyngeal carcinoma (NPC), demonstrates spontaneous lytic replication and high-titer virus production in comparison to the prototype B95-8 EBV strain. Genetic comparisons of M81 and B95-8 EBVs were previously been performed in order to determine if the hyperlytic property of M81 is associated with sequence differences in essential lytic genes. EBV SM is an RNA-binding protein expressed during early lytic replication that is essential for virus production. We compared the functions of M81 SM and B95-8 SM and demonstrate that polymorphisms in SM do not contribute to the lytic phenotype of M81 EBV. However, the expression level of the EBV DNA polymerase protein was much higher in M81- than in B95-8-infected cells. The relative deficiency in the expression of B95-8 DNA polymerase was related to the B95-8 genome deletion, which truncates the BALF5 3′ untranslated region (UTR). Similarly, the insertion of bacmid DNA into the widely used recombinant B95-8 bacmid creates an inefficient BALF5 3′ UTR. We further showed that the while SM is required for and facilitates the efficient expression of both M81 and B95-8 mRNAs regardless of the 3′ UTR, the BALF5 3′ UTR sequence is important for BALF5 protein translation. These data indicate that the enhanced lytic replication and virus production of M81 compared to those of B95-8 are partly due to the robust translation of EBV DNA polymerase required for viral DNA replication due to a more efficient BALF5 3′ UTR in M81.IMPORTANCEEpstein-Barr virus (EBV) infects more than 90% of the human population, but the incidence of EBV-associated tumors varies greatly in different parts of the world. Thus, understanding the connection between genetic polymorphisms from patient isolates of EBV, gene expression phenotypes, and disease is important and may help in developing antiviral therapy. This study examines potential causes of the enhanced lytic replicative properties of M81 EBV isolated from a nasopharyngeal carcinoma (NPC) patient and provides new evidence for the role of the BALF5 gene 3′ UTR sequence in DNA polymerase protein expression during lytic replication. Variation in the gene structure of the DNA polymerase gene may therefore contribute to lytic virus reactivation and pathogenesis.

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