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Zerbib D, Prentki P, Gamas P, et al. Functional organization of the ends of IS 1: specific binding site for an IS1-encoded protein. Mol Microbiol. 1990;4(9):1477-1486doi: 10.1111/j.1365-2958.1990.tb02058.x.
Zerbib, D., Prentki, P., Gamas, P., Freund, E., Galas, D. J., & Chandler, M. (1990). Functional organization of the ends of IS 1: specific binding site for an IS1-encoded protein. Molecular microbiology, 4(9), 1477-1486. https://doi.org/10.1111/j.1365-2958.1990.tb02058.x
Zerbib, D, et al. "Functional organization of the ends of IS 1: specific binding site for an IS1-encoded protein." Molecular microbiology vol. 4,9 (1990): 1477-1486. doi: https://doi.org/10.1111/j.1365-2958.1990.tb02058.x
Zerbib D, Prentki P, Gamas P, Freund E, Galas DJ, Chandler M. Functional organization of the ends of IS 1: specific binding site for an IS1-encoded protein. Mol Microbiol. 1990 Sep;4(9):1477-1486. doi: 10.1111/j.1365-2958.1990.tb02058.x. PMID: 28776821.
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Mol Microbiol. 1990 Sep;4(9):1477-1486. doi: 10.1111/j.1365-2958.1990.tb02058.x.

Functional organization of the ends of IS 1: specific binding site for an IS1-encoded protein.

Molecular microbiology

D Zerbib, P Prentki, P Gamas, E Freund, D J Galas, M Chandler

Affiliations

  1. Centre de Recherche de Biochimie et Génétique Cellulaire du CNRS, 118 route de Narbonne. 31062 Toulouse Cedex, France.Déapartement de Biologie Moléculaire, Université de Genève, 1211 Genève 4, SwitzerlandMolecular Biology, University of Southern California, Los Angeles, California 90089-1481, USA.

PMID: 28776821 DOI: 10.1111/j.1365-2958.1990.tb02058.x

Abstract

The IS 1-encoded protein InsA binds specifically to both ends of IS 1, and acts as a repressor of IS1 gene expression and may be a direct inhibitor of the transposition process. We show here, using DNasel 'foot-printing' and gel retardation, that the InsA binding sites are located within the 24/25bp minimal active ends of IS1 and that InsA induces DNA bending upon binding. Conformational modification of the ends of IS 1 as a result of binding of the host protein integration host factor (IHF) to its site within the minimal ends has been previously observed. Using a collection of synthetic mutant ends we have mapped some of the nucleotide sequence requirements for InsA binding and for transposition activity. We show that sequences necessary for InsA binding are also essential for transposition activity. We demonstrate that InsA and IHF binding sites overlap since some sequence determinants are shared by both InsA and IHF. The data suggest that these ends contain two functional domains: one for binding of InsA and IHF, and the other for transposition activity. A third region, when present, may enhance transposition activity with an intact right end. This 'architecture' of the ends of IS 1 is remarkably similar to that of IS elements IS10, IS50 and IS903.

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