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- W1981844364 abstract "X-ray cocrystal structures of Tn5 transposase (Tnp) bound to its 19 base pair (bp) recognition end sequence (ES) reveal contacts between a β-loop (amino acids 240−260) and positions 3, 4, 5, and 6 of the ES. Here, we show that mutations of residues in this loop affect both in vivo and in vitro transposition. Most mutations are detrimental, whereas some mutations at position 242 cause hyperactivity. More specifically, mutations to the β-loop affect every individual step of transposition tested. Mutants performing in vivo and in vitro transposition less efficiently also form fewer synaptic complexes, whereas hyperactive Tnps form more synaptic complexes. Surprisingly, two hypoactive mutations, K244R and R253L, also affect the cleavage steps of transposition with a much more dramatic effect on the second double end break (DEB) complex formation step, indicating that the β-loop likely plays an important roll in positioning the substrate DNA within the catalytic site. Finally, all mutants tested decrease efficiency of the final transposition step, strand transfer. A disparity in cleavage rate constants in vitro for mutants with changes to the proline at position 242 on transposons flanked by ESs differing in the orientation of the A−T base pair at position 4 allows us to postulate that P242 contacts the position 4 nucleotide pair. On the basis of these data, we propose a sequential model for end cleavage in Tn5 transposition in which the uncleaved PEC is not symmetrical, and conformational changes are necessary between the first and second cleavage events and also for the final strand transfer step of transposition." @default.
- W1981844364 created "2016-06-24" @default.
- W1981844364 creator A5041494111 @default.
- W1981844364 creator A5056130741 @default.
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- W1981844364 date "2006-12-01" @default.
- W1981844364 modified "2023-09-27" @default.
- W1981844364 title "Mutation of Tn5Transposase β-Loop Residues Affects All Steps of Tn5Transposition: The Role of Conformational Changes in Tn5Transposition†" @default.
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- W1981844364 doi "https://doi.org/10.1021/bi061227v" @default.
- W1981844364 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2597523" @default.
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