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Applied and Environmental Microbiology, January 2006, p. 291-297, Vol. 72, No. 1
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.1.291-297.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Functional Analysis of Unique Class II Insertion Sequence IS1071

Masahiro Sota,^1,2* Hirokazu Yano,² Yuji Nagata,² Yoshiyuki Ohtsubo,² Hiroyuki Genka,² Hisashi Anbutsu,^2, Haruhiko Kawasaki,³ and Masataka Tsuda²

Department of Environmental Simulation, Institute for Environmental Sciences, Rokkasho, Aomori 039-3212,¹ Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, Katahira, Sendai 980-8577,² Department of Applied Biochemistry, Graduate School of Agriculture and Biological Sciences, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan³

Received 20 June 2005/ Accepted 29 September 2005

Various xenobiotic-degrading genes on many catabolic plasmids are often flanked by two copies of an insertion sequence, IS1071. This 3.2-kb IS element has long (110-bp) terminal inverted repeats (IRs) and a transposase gene that are phylogenetically related to those of the class II transposons. However, the transposition mechanism of IS1071 has remained unclear. Our study revealed that IS1071 was only able to transpose at high frequencies in two environmental ß-proteobacterial strains, Comamonas testosteroni and Delftia acidovorans, and not in any of the bacteria examined which belong to the - and -proteobacteria. IS1071 was found to have the functional features of the class II transposons in that (i) the final product of the IS1071 transposition was a cointegrate of its donor and target DNA molecules connected by two directly repeated copies of IS1071, one at each junction; (ii) a 5-bp duplication of the target sequence was observed at the insertion site; and (iii) a tnpA mutation of IS1071 was efficiently complemented by supplying the wild-type tnpA gene in trans. Deletion analysis of the IS1071 IR sequences indicated that nearly the entire region of the IRs was required for its transposition, suggesting that the interaction between the transposase and IRs of IS1071 might be different from that of the other well-characterized class II transposons.

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* Corresponding author. Present address: Department of Biological Sciences, 222 Life Sciences North, University of Idaho, Moscow, ID 83844-3051. Phone: (208) 885-4031. Fax: (208) 885-7905. E-mail: sota{at}uidaho.edu

Present address: Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), Higashi 1-1-1, Tsukuba, Ibaraki 305-8566, Japan.

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Applied and Environmental Microbiology, January 2006, p. 291-297, Vol. 72, No. 1
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.1.291-297.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

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