A novel DNA nuclease is stimulated by association with the GINS complex.

Research paper by Zhuo Z Li, Miao M Pan, Thomas J TJ Santangelo, Wiebke W Chemnitz, Wei W Yuan, James L JL Edwards, Jerard J Hurwitz, John N JN Reeve, Zvi Z Kelman

Indexed on: 05 Apr '11Published on: 05 Apr '11Published in: Nucleic acids research


Chromosomal DNA replication requires the spatial and temporal coordination of the activities of several complexes that constitute the replisome. A previously uncharacterized protein, encoded by TK1252 in the archaeon Thermococcus kodakaraensis, was shown to stably interact with the archaeal GINS complex in vivo, a central component of the archaeal replisome. Here, we document that this protein (TK1252p) is a processive, single-strand DNA-specific exonuclease that degrades DNA in the 5' → 3' direction. TK1252p binds specifically to the GINS15 subunit of T. kodakaraensis GINS complex and this interaction stimulates the exonuclease activity in vitro. This novel archaeal nuclease, designated GINS-associated nuclease (GAN), also forms a complex in vivo with the euryarchaeal-specific DNA polymerase D. Roles for GAN in replisome assembly and DNA replication are discussed.