Structural and functional analyses of mutant Fur proteins with impaired regulatory function.
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.
Wertheimer
A M
AM
Department of Molecular Microbiology and Immunology, School of Medicine, Oregon Health Sciences University, Portland 97201-3098.
Tolmasky
M E
ME
Actis
L A
LA
Crosa
J H
JH
D001426:Bacterial Proteins / Q000737:chemistry*; D001483:Base Sequence; D003001:Cloning, Molecular; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D005816:Genetic Complementation Test; D007501:Iron / Q000378:metabolism; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012097:Repressor Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship; D014733:Vibrio / Q000235:genetics*
D001426:Bacterial Proteins; D012097:Repressor Proteins; C068477:ferric uptake regulating proteins, bacterial; D007501:Iron