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Published in

American Society for Microbiology, Journal of Bacteriology, 16(176), p. 5116-5122, 1994

DOI: 10.1128/jb.176.16.5116-5122.1994

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Structural and functional analyses of mutant Fur proteins with impaired regulatory function.

Journal article published in 1994 by A. M. Wertheimer, M. E. Tolmasky ORCID, L. A. Actis, J. H. Crosa
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Vibrio anguillarum Fur mutants, 775met9 and 775met11, were characterized. V. anguillarum 775met9 had a change of D to G at position 104 located in the carboxy terminus resulting in impaired Fur activity. Computer analysis predicts perturbation of an alpha-helix in the carboxy terminus which may interfere with Fur protein conformation. Strain 775met11 had a change in the start codon resulting in no protein synthesis. The mutants are unstable, and reversion to the wild type occurs frequently.