Primer Length Dependence of Binding of DNA Polymerase I Klenow Fragment to Template−Primer Complexes Containing Site-Specific Bulky Lesions†

Biochemistry ◽  
1999 ◽  
Vol 38 (36) ◽  
pp. 11834-11843 ◽  
Author(s):  
Olga Rechkoblit ◽  
Shantu Amin ◽  
Nicholas E. Geacintov
Author(s):  
Devendranath Simha ◽  
Deepmala Yadav ◽  
Robert W. Rzepka ◽  
Vaseem A. Palejwala ◽  
M. Zafri Humayun

Biochemistry ◽  
1984 ◽  
Vol 23 (9) ◽  
pp. 2073-2078 ◽  
Author(s):  
Anup K. Hazra ◽  
Sevilla Detera-Wadleigh ◽  
Samuel H. Wilson

Author(s):  
Morgan E. Milton ◽  
Jun-yong Choe ◽  
Richard B. Honzatko ◽  
Scott W. Nelson

Infection by the parasitePlasmodium falciparumis the leading cause of malaria in humans. The parasite has a unique and essential plastid-like organelle called the apicoplast. The apicoplast contains a genome that undergoes replication and repair through the action of a replicative polymerase (apPOL). apPOL has no direct orthologs in mammalian polymerases and is therefore an attractive antimalarial drug target. No structural information exists for apPOL, and the Klenow fragment ofEscherichia coliDNA polymerase I, which is its closest structural homolog, shares only 28% sequence identity. Here, conditions for the crystallization of and preliminary X-ray diffraction data from crystals ofP. falciparumapPOL are reported. Data complete to 3.5 Å resolution were collected from a single crystal (2 × 2 × 5 µm) using a 5 µm beam. The space groupP6522 (unit-cell parametersa=b= 141.8,c= 149.7 Å, α = β = 90, γ = 120°) was confirmed by molecular replacement. Refinement is in progress.


1998 ◽  
Vol 278 (1) ◽  
pp. 147-165 ◽  
Author(s):  
Mekbib Astatke ◽  
Nigel D.F Grindley ◽  
Catherine M Joyce

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