A1 Refereed original research article in a scientific journal
DIVISION-OF-LABOR AMONG MONOMERS WITHIN THE MU-TRANSPOSASE TETRAMER
Authors: BAKER TA, MIZUUCHI M, SAVILAHTI H, MIZUUCHI K
Publisher: CELL PRESS
Publication year: 1993
Journal:: Cell
Journal name in source: CELL
Journal acronym: CELL
Volume: 74
Issue: 4
First page : 723
Last page: 733
Number of pages: 11
ISSN: 0092-8674
DOI: https://doi.org/10.1016/0092-8674(93)90519-V
Abstract
A single tetramer of Mu transposase (MuA) pairs the recombination sites, cleaves the donor DNA, and joins these ends to a target DNA by strand transfer. Analysis of C-terminal deletion derivatives of MuA reveals that a 30 amino acid region between residues 575 and 605 is critical for these three steps. Although inactive on its own, a deletion protein lacking this region assembles with the wild-type protein. These mixed tetramers carry out donor cleavage but do not promote strand transfer, even when the donor cleavage stage is by-passed. These data suggest that the active center of the transposase is composed of the C-terminus of four MuA monomers; one dimer carries out donor cleavage while all four monomers contribute to strand transfer.
A single tetramer of Mu transposase (MuA) pairs the recombination sites, cleaves the donor DNA, and joins these ends to a target DNA by strand transfer. Analysis of C-terminal deletion derivatives of MuA reveals that a 30 amino acid region between residues 575 and 605 is critical for these three steps. Although inactive on its own, a deletion protein lacking this region assembles with the wild-type protein. These mixed tetramers carry out donor cleavage but do not promote strand transfer, even when the donor cleavage stage is by-passed. These data suggest that the active center of the transposase is composed of the C-terminus of four MuA monomers; one dimer carries out donor cleavage while all four monomers contribute to strand transfer.
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