Sequence analysis of termini of conjugative transposon Tn916

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Sequence analysis of termini of conjugative transposon Tn916.

Transposon Tn916 is a 16.4-kilobase, broad-host-range, conjugative transposon originally identified on the chromosome of Enterococcus (Streptococcus) faecalis DS16. Its termini have been sequenced along with the junction regions for two different insertions. The ends were found to contain imperfect inverted repeat sequences with identity at 20 of 26 nucleotides. Further in from the ends, imperf...

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An intermediate in transposition of the conjugative transposon Tn916.

Using the conjugative transposon Tn916, we have identified a closed covalent circular form produced in vivo that is able to serve as an intermediate in transposition. When a region of a streptococcal chromosome containing Tn916 is cloned in an Escherichia coli plasmid, supercoiled transposon molecules are excised spontaneously. The purified supercoiled forms transform Bacillus subtilis protopla...

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Specific binding of integrase to the origin of transfer (oriT) of the conjugative transposon Tn916.

Purified integrase protein (Int) of the conjugative transposon Tn916 was shown, using nuclease protection experiments, to bind specifically to a site within the origin of conjugal transfer of the transposon, oriT. A sequence similar to the ends of the transposon that are bound by the C-terminal DNA-binding domain of Int was present in the protected region. However, Int binding to oriT required ...

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Conjugative transposition of Tn916 requires the excisive and integrative activities of the transposon-encoded integrase.

Transposon Tn916 is a 16.4-kb broad-host-range conjugative transposon originally detected in the chromosome of Enterococcus faecalis DS16. Transposition of Tn916 and related transposons involves excision of a free, nonreplicative, covalently closed circular intermediate that is substrate for integration. Excisive recombination requires two transposon-encoded proteins, Xis-Tn and Int-Tn, whereas...

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Interactions of the integrase protein of the conjugative transposon Tn916 with its specific DNA binding sites.

The binding of two chimeric proteins, consisting of the N-terminal or C-terminal DNA binding domain of Tn916 Int fused to maltose binding protein, to specific oligonucleotide substrates was analyzed by gel mobility shift assay. The chimeric protein with the N-terminal domain formed two complexes of different electrophoretic mobilities. The faster-moving complex, whose formation displayed no coo...

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1988

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.170.7.3046-3052.1988