Y-family DNA polymerase
catalyses translesion synthesis and interacts functionally with PCNA2
シロイヌナズナのYファミリーDNAポリメラーゼ
は損傷乗り越え複製を触媒し、PCNA2と機能的に相互作用する
Anderson, H.*; Vonarx, E.*; Pastushok, L.*; 中川 繭; 片渕 淳*; Gruz, P.*; Rubbo, A.*; Grice, D.*; Osmond, M.*; 坂本 綾子; 能美 健彦*; Xiao, W.*; Kunz, B.*
Anderson, H.*; Vonarx, E.*; Pastushok, L.*; Nakagawa, Mayu; Katafuchi, Atsushi*; Gruz, P.*; Rubbo, A.*; Grice, D.*; Osmond, M.*; Sakamoto, Ayako; Nomi, Takehiko*; Xiao, W.*; Kunz, B.*
We assessed the roles of
and
in TLS mediated UV resistance.
defective mutants sensitized growth of roots and whole plants to UV radiation indicating AtPol
contributes to UV resistance.
alone did not complement the UV sensitivity conferred by deletion of yeast
, although AtPol
exhibited cyclobutane dimer bypass activity and interacted with yeast PCNA in vitro. Co-expression of
and
, but not
, restored normal UV resistance and mutation kinetics in the
mutant. A single residue difference at site 201, which lies adjacent to the lysine ubiquitylated in PCNA, appeared responsible for the inability of PCNA1 to function with AtPol
in UV treated yeast. PCNA interacting protein boxes and an ubiquitin-binding motif in AtPol
were found to be required for restoration of UV resistance in the
mutant by
and
. These observations indicate AtPol
can catalyse TLS past UV induced DNA damage, and link the biological activity of AtPol
in UV irradiated cells to PCNA2 and PCNA-and ubiquitin-binding motifs in AtPol
.