The terminal protein of the linear DNA plasmid pGKL2 shares an N-terminal domain of the plasmid-encoded DNA polymerase

Yeast ◽  
1996 ◽  
Vol 12 (3) ◽  
pp. 241-246 ◽  
Author(s):  
Masaharu Takeda ◽  
Hiroyuki Hiraishi ◽  
Toshikazu Takesako ◽  
Sumio Tanase ◽  
Norio Gunge
Keyword(s):  
Dna Polymerase ◽  
Terminal Protein ◽  
Linear Dna ◽  
Terminal Domain ◽  
Dna Plasmid

ø29 DNA polymerase requires the N-terminal domain to bind terminal protein and DNA primer substrates

1998 ◽  
Vol 278 (4) ◽  
pp. 741-755 ◽  
Author(s):  
Verónica Truniger ◽  
José M Lázaro ◽  
Margarita Salas ◽  
Luis Blanco
Keyword(s):  
Dna Polymerase ◽  
Terminal Protein ◽  
Terminal Domain

scholarly journals Secretion of killer toxin encoded on the linear DNA plasmid pGKL1 from Saccharomyces cerevisiae.

1990 ◽  
Vol 265 (28) ◽  
pp. 17274-17280
Author(s):  
M Tokunaga ◽  
A Kawamura ◽  
K Kitada ◽  
F Hishinuma
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Killer Toxin ◽  
Linear Dna ◽  
Dna Plasmid

scholarly journals The Loop of the TPR1 Subdomain of Phi29 DNA Polymerase Plays a Pivotal Role in Primer-Terminus Stabilization at the Polymerization Active Site

Biomolecules ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 648
Author(s):  
del Prado ◽  
Santos ◽  
Lázaro ◽  
Salas ◽  
de Vega
Keyword(s):  
Dna Polymerase ◽  
Active Site ◽  
Structural Changes ◽  
Binding Capacity ◽  
Dna Polymerases ◽  
Crystallographic Structure ◽  
Genome Replication ◽  
Terminal Protein ◽  
Phi29 Dna Polymerase

Bacteriophage Phi29 DNA polymerase belongs to the protein-primed subgroup of family B DNA polymerases that use a terminal protein (TP) as a primer to initiate genome replication. The resolution of the crystallographic structure showed that it consists of an N-terminal domain with the exonuclease activity and a C-terminal polymerization domain. It also has two subdomains specific of the protein-primed DNA polymerases; the TP Regions 1 (TPR1) that interacts with TP and DNA, and 2 (TPR2), that couples both processivity and strand displacement to the enzyme. The superimposition of the structures of the apo polymerase and the polymerase in the polymerase/TP heterodimer shows that the structural changes are restricted almost to the TPR1 loop (residues 304–314). In order to study the role of this loop in binding the DNA and the TP, we changed the residues Arg306, Arg308, Phe309, Tyr310, and Lys311 into alanine, and also made the deletion mutant Δ6 lacking residues Arg306–Lys311. The results show a defective TP binding capacity in mutants R306A, F309A, Y310A, and Δ6. The additional impaired primer-terminus stabilization at the polymerization active site in mutants Y310A and Δ6 allows us to propose a role for the Phi29 DNA polymerase TPR1 loop in the proper positioning of the DNA and TP-priming 3’-OH termini at the preinsertion site of the polymerase to enable efficient initiation and further elongation steps during Phi29 TP-DNA replication.

Insights into the mechanism of the β-elimination catalyzed by the N-terminal domain of DNA polymerase β

Tetrahedron ◽  
1997 ◽  
Vol 53 (35) ◽  
pp. 12057-12066 ◽  
Author(s):  
Gregory P. Mullen ◽  
Walfrido Antuch ◽  
Mark W. Maciejewski ◽  
Rajendra Prasad ◽  
Samuel H. Wilson
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Β ◽  
Terminal Domain

scholarly journals Data on multimerization efficiency for short linear DNA templates and phosphoryl guanidine primers during isothermal amplification with Bst exo- DNA polymerase

Data in Brief ◽  
2020 ◽  
Vol 29 ◽  
pp. 105188 ◽  
Author(s):  
Ravil R. Garafutdinov ◽  
Assol R. Sakhabutdinova ◽  
Maxim S. Kupryushkin ◽  
Dmitrii V. Pyshnyi
Keyword(s):  
Dna Polymerase ◽  
Isothermal Amplification ◽  
Dna Templates ◽  
Linear Dna
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