Phenylalanine 171 is a molecular brake for translesion synthesis across benzo[a]pyrene-guanine adducts by human DNA polymerase kappa

Author(s):  
Akira Sassa ◽  
Naoko Niimi ◽  
Hirofumi Fujimoto ◽  
Atsushi Katafuchi ◽  
Petr Grúz ◽  
...  
2004 ◽  
Vol 9 (12) ◽  
pp. 1139-1150 ◽  
Author(s):  
Rika Kusumoto ◽  
Chikahide Masutani ◽  
Shizu Shimmyo ◽  
Shigenori Iwai ◽  
Fumio Hanaoka

2002 ◽  
Vol 278 (2) ◽  
pp. 784-790 ◽  
Author(s):  
Irina G. Minko ◽  
M. Todd Washington ◽  
Manorama Kanuri ◽  
Louise Prakash ◽  
Satya Prakash ◽  
...  

Biochemistry ◽  
2002 ◽  
Vol 41 (19) ◽  
pp. 6100-6106 ◽  
Author(s):  
Naomi Suzuki ◽  
Eiji Ohashi ◽  
Alexander Kolbanovskiy ◽  
Nicholas E. Geacintov ◽  
Arthur P. Grollman ◽  
...  

2005 ◽  
Vol 280 (48) ◽  
pp. 39684-39692 ◽  
Author(s):  
Dominic Chiapperino ◽  
Mangmang Cai ◽  
Jane M. Sayer ◽  
Haruhiko Yagi ◽  
Heiko Kroth ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Olga Rechkoblit ◽  
Robert E. Johnson ◽  
Yogesh K. Gupta ◽  
Louise Prakash ◽  
Satya Prakash ◽  
...  

AbstractPrimPol is a human DNA polymerase-primase that localizes to mitochondria and nucleus and bypasses the major oxidative lesion 7,8-dihydro-8-oxoguanine (oxoG) via translesion synthesis, in mostly error-free manner. We present structures of PrimPol insertion complexes with a DNA template-primer and correct dCTP or erroneous dATP opposite the lesion, as well as extension complexes with C or A as a 3′−terminal primer base. We show that during the insertion of C and extension from it, the active site is unperturbed, reflecting the readiness of PrimPol to accommodate oxoG(anti). The misinsertion of A opposite oxoG(syn) also does not alter the active site, and is likely less favorable due to lower thermodynamic stability of the oxoG(syn)•A base-pair. During the extension step, oxoG(syn) induces an opening of its base-pair with A or misalignment of the 3′-A primer terminus. Together, the structures show how PrimPol accurately synthesizes DNA opposite oxidatively damaged DNA in human cells.


Sign in / Sign up

Export Citation Format

Share Document