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A more recent version of this article appeared on December 6, 2002
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M206889200v1
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Papers In Press, published online ahead of print October 3, 2002
J. Biol. Chem, 10.1074/jbc.M206889200
Submitted on July 10, 2002
Revised on October 3, 2002
Accepted on October 3, 2002

Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis

Giovanni Maga, Giuseppe Villani, Kristijan Ramadan, Igor Shevelev, Nicolas Tanguy le Gac, Luis Blanco, Giuseppina Blanca, Silvio Spadari, and Ulrich Hubscher

DNA Enzymology and Molecular Virology, Ist. di Genetica Molecolare -IGM C.N.R., Pavia, Pavia I-27100

Corresponding Author: maga{at}igm.cnr.it

Proliferating cell nuclear antigen (PCNA) has been shown to interact with a variety of DNA polymerases (pol) such as pol delta , pol epsilon , pol iota , pol kappa , pol eta and pol beta . Here we show that PCNA directly interacts with the newly discovered pol lambda cloned from human cells. This interaction stabilizes the binding of pol lambda to the primer template thus increasing its affinity for the hydroxyl primer and its processivity in DNA synthesis, but no effect of PCNA was detected on the rate of nucleotide incorporation or discrimination efficiency by pol lambda . PCNA was found to stimulate efficient synthesis by pol lambda across an abasic site (AP site). When compared with pol lambda , human pol lambda showed the ability to incorporate a nucleotide in front of the lesion. Addition of PCNA led to efficient elongation past the AP site by pol lambda but not by pol delta .However, when tested on a template containing a bulky DNA lesion, such as the major cisplatin Pt-d(GpG)adduct, PCNA could not allow translesion synthesis by pol lambda . Our results suggest that the complex between PCNA and pol lambda may play an important role in the bypass of abasic sites in human cells.


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