Journal of Bacteriology, May 2001, p. 2970-2970, Vol. 183, No. 9
Rubrerythrin and Rubredoxin Oxidoreductase in Desulfovibrio
vulgaris: a Novel Oxidative Stress Protection System
Departments of Chemistry and Microbiology and Center for
Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602, and Department of Biological Sciences, University of Calgary, Calgary,
Alberta T2N IN4, Canada
Volume 183, no. 1, p. 101-108, 2001. Page 104, Fig. 2: The
deduced amino acid sequence of a putative iron or manganese-containing superoxide dismutase (Fe/Mn-SOD) from Desulfovibrio vulgaris
differs from that in a more recent (but still unfinished) D. vulgaris genome sequence on The Institute for Genomic Research
(TIGR) web page (updated Dec. 10, 2000). A revised Fig. 2 incorporating
the TIGR-derived amino acid sequence for the D. vulgaris SOD
homolog is shown below (labeled Dv). The updated residue 8 (in bold)
results in a double-arginine motif characteristic of signal peptides in other bacterial redox proteins. The updated sequence reinforces our
original suggestion that the mature Fe/Mn-SOD homolog in D. vulgaris would be periplasmic.
0021-9193/01 DOI:
Copyright © 2001, American Society for Microbiology. All rights reserved.
AUTHOR'S CORRECTION

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