Removal of 3'-OH-terminal nucleotides from blunt-ended long terminal repeat termini by the avian retrovirus integration protein.
The avian myeloblastosis virus integration protein (IN) was capable of removing a specific set of 3'-OH-terminal nucleotides from blunt-ended long terminal repeat (LTR) substrates which resembled linear viral DNA in vivo. The 3'-OH-recessed ends map to the in vivo site of integration on linear viral DNA. The linear DNA plasmid substrate was formed by the generation of a unique DraI restriction enzyme site (TTT/AAA) at the circle junction of a 330-bp tandem LTR-LTR insert. IN preferentially released the three T nucleotides from the minus strand of the U3 LTR substrate compared with its ability to remove the three T nucleotides from the plus strand of the U5 LTR substrate. It was also observed that IN was capable of cleaving a non-LTR DNA substrate containing sequence homology to the U5 LTR terminus.
Vora
A C
AC
Institute for Molecular Virology, St. Louis University Medical Center, Missouri 63110.
Fitzgerald
M L
ML
Grandgenett
D P
DP
D009189:Avian Myeloblastosis Virus / Q000235:genetics*; D001483:Base Sequence; D002472:Cell Transformation, Viral; D004254:DNA Nucleotidyltransferases / Q000502:physiology*; D066298:In Vitro Techniques; D019426:Integrases; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008969:Molecular Sequence Data; D010957:Plasmids; D011995:Recombination, Genetic; D012091:Repetitive Sequences, Nucleic Acid; D013379:Substrate Specificity
D008345:Manganese; D004254:DNA Nucleotidyltransferases; D019426:Integrases; D008274:Magnesium