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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.