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

Li, Zhuo, Pan, Miao, Santangelo, Thomas J., Chemnitz, Wiebke, Yuan, Wei, Edwards, James L., Hurwitz, Jerard, Reeve, John N., Kelman, Zvi
Nucleic acids research 2011 v.39 no.14 pp. 6114-6123
DNA, DNA replication, DNA-directed DNA polymerase, Thermococcus kodakarensis
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' [rightward arrow] 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.