Identification of the coding sequence for herpes simplex virus uracil-DNA glycosylase.
نویسندگان
چکیده
We have recently isolated a herpes simplex virus (HSV) type 2 (strain 333)-specific cDNA that encodes uracil-DNA glycosylase. This cDNA lies between 0.065 and 0.08 map units on the HSV genome. Within this region there are five overlapping transcripts which encompass three open reading frames. We have determined that the second open reading frame, UL-2, codes for glycosylase. In vitro transcription of the UL-2 region and subsequent translation yielded uracil-DNA glycosylase activity. Sequence analysis of the UL-2 open reading frame indicated a coding capacity of 295 amino acids. Comparison to the HSV type 1 (strain 17) sequence indicated that there is 74% amino acid homology between the two strains, with most of the conservation occurring in the middle and the 3' end. The 5' end, however, has diverged considerably.
منابع مشابه
Gene UL2 of herpes simplex virus type 1 encodes a uracil-DNA glycosylase.
An insertion mutant of herpes simplex virus type 1 has been constructed which carries the lacZ gene from Escherichia coli within the coding sequence of gene UL2, which is in the long unique region of the genome. In a one-step growth curve experiment this recombinant (called in 1601) grew as well as the wild-type (wt) parent virus, indicating that the UL2 gene is dispensable for growth in tissue...
متن کاملIdentification of human herpesvirus 6 uracil-DNA glycosylase gene.
Uracil-DNA glycosylase encoded in many species functions as a DNA repair enzyme that removes uracil residues from DNA. To investigate the potential function of uracil-DNA glycosylase encoded by human herpes-virus 6 (HHV-6), we sequenced a DNA clone (pSTY09), identified an open reading frame of 765 bp and compared the putative amino acid sequence with other uracil-DNA glycosylases, by computer a...
متن کاملA kinetic analysis of substrate recognition by uracil-DNA glycosylase from herpes simplex virus type 1.
Uracil-DNA glycosylase (UDG) is responsible for the removal of uracil from DNA. It has previously been demonstrated that UDG exhibits some sequence dependence in its activity, although this has not been well characterised. This study has investigated the sequence-dependent activity of UDG from herpes simplex virus type-1 (HSV-1). A more detailed analysis has been possible by using both kinetic ...
متن کاملHerpes simplex virus type 1 uracil-DNA glycosylase: isolation and selective inhibition by novel uracil derivatives.
We have purified Herpes simplex type 1 (HSV1) uracil-DNA glycosylase from the nuclei of HSV1-infected HeLa cells harvested 8 h post-infection, at which time the induction of the enzyme is a maximum. The enzyme has been shown to be distinct from the host enzyme, isolated from HeLa cells, by its lack of sensitivity to a monoclonal antibody to human uracil-DNA glycosylase. Furthermore, several ura...
متن کاملAssociation between the herpes simplex virus-1 DNA polymerase and uracil DNA glycosylase.
Herpes simplex virus-1 (HSV-1) is a large dsDNA virus that encodes its own DNA replication machinery and other enzymes involved in DNA transactions. We recently reported that the HSV-1 DNA polymerase catalytic subunit (UL30) exhibits apurinic/apyrimidinic and 5'-deoxyribose phosphate lyase activities. Moreover, UL30, in conjunction with the viral uracil DNA glycosylase (UL2), cellular apurinic/...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Journal of virology
دوره 62 12 شماره
صفحات -
تاریخ انتشار 1988