Mutagenesis of human DNA polymerase lambda: essential roles of Tyr505 and Phe506 for both DNA polymerase and terminal transferase activities.
DNA polymerase (pol) lambda is homologous to pol beta and has intrinsic polymerase and terminal transferase activities. However, nothing is known about the amino acid residues involved in these activities. In order to precisely define the nucleotide-binding site of human pol lambda, we have mutageni...
Main Authors: | Shevelev, I, Blanca, G, Villani, G, Ramadan, K, Spadari, S, Hübscher, U, Maga, G |
---|---|
Formato: | Journal article |
Idioma: | English |
Publicado em: |
2003
|
Registos relacionados
-
De novo DNA synthesis by human DNA polymerase lambda, DNA polymerase mu and terminal deoxyribonucleotidyl transferase.
Por: Ramadan, K, et al.
Publicado em: (2004) -
Human DNA polymerase lambda diverged in evolution from DNA polymerase beta toward specific Mn(++) dependence: a kinetic and thermodynamic study.
Por: Blanca, G, et al.
Publicado em: (2003) -
DNA elongation by the human DNA polymerase lambda polymerase and terminal transferase activities are differentially coordinated by proliferating cell nuclear antigen and replication protein A.
Por: Maga, G, et al.
Publicado em: (2005) -
Human DNA polymerases lambda and beta show different efficiencies of translesion DNA synthesis past abasic sites and alternative mechanisms for frameshift generation.
Por: Blanca, G, et al.
Publicado em: (2004) -
The human DNA polymerase lambda interacts with PCNA through a domain important for DNA primer binding and the interaction is inhibited by p21/WAF1/CIP1.
Por: Maga, G, et al.
Publicado em: (2004)