期刊
JOURNAL OF BACTERIOLOGY
卷 190, 期 4, 页码 1484-1487出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.01488-07
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- NIGMS NIH HHS [GM50693] Funding Source: Medline
A series of Tn5 transposases (Tnp's) with mutations at the conserved amino acid position W450, which was structurally predicted to be important for synapsis, have been generated and characterized. This study demonstrates that W450 is involved in hydrophobic (and possibly aromatic) contacts within the Tnp monomer that negatively regulate synaptic complex formation.
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