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The Herpes simplex virus‐1 DNA polymerase exhibits 3′ phosphatase activity
Author(s) -
Ravi Rupesh Kanchi,
Boehmer Paul E.
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.lb51
Subject(s) - ap site , ap endonuclease , dna glycosylase , base excision repair , dna polymerase , exonuclease , dna repair , uracil dna glycosylase , dna , biology , microbiology and biotechnology , dna replication , dna ligase , biochemistry , chemistry
Herpes simplex virus‐1 (HSV‐1) is a large dsDNA virus that encodes its own DNA replication machinery, including enzymes involved in nucleotide metabolism. We recently demonstrated that the HSV‐1 DNA polymerase (UL30) exhibits AP and 5′ dRP lyase activities. Moreover, UL30 in conjunction with the viral uracil DNA glycosylase as well as cellular AP endonuclease and DNA ligase IIIα/XRCC1, perform uracil‐initiated Base Excision Repair (BER). As an alternative route to repairing base adducts and abasic sites, and as a mechanism to process ssDNA breaks we have investigated the ability of UL30 to process various 3′ ends. Interestingly, we find that UL30 can degrade 3′ sugar phosphate as well as 3′ phosphate terminated DNA. Moreover, UL30 exhibits a 3′ phosphatase activity that removes 3′ phosphate prior to 3′–5′ exonuclease action. These novel activities would allow UL30 to process AP sites following β‐elimination though incision by its inherent AP lyase activity or DNA breaks that result in 3′ phosphate terminated DNA following βδ‐elimination or X‐ray irradiation. Further studies will investigate how UL30 can repair this damage in conjunction with other factors. These findings further highlight the role of DNA repair in the maintenance of a viral genome with implications on both lytic replication and reactivation from latency. This work was supported by grant GM 062643 from the NIH.