Ty1 retrotransposition in Saccharomyces
cerevisiae requires integrase (IN)-mediated insertion of Ty1 cDNA
into the host genome. The transposition components are assembled in the
cytoplasm and must cross the nuclear envelope to reach the genomic
target since the yeast cell nuclear membrane remains intact throughout
the cell cycle. We have identified a bipartite nuclear localization
signal (NLS) in IN that directs IN to the nucleus and is required for
Ty1 transposition. Mutations in the NLS that specifically abolish
nuclear localization inactivate transpositional integration but do not
affect reverse transcription, protein processing, or catalytic activity
in vitro. No additional Ty1-encoded proteins are required for IN nuclear
localization. Intragenic complementation experiments suggest that Ty1 IN
functions as a multimer and contains at least two distinct domains, one
required for strand transfer and the other for nuclear localization.
This research was sponsored by the National Cancer Institute under a
contract with ABL.
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