Characterization of the gene encoding Superoxide dismutase of Bordetella pertussis and construction of a SOD-deficient mutant

The Bordetella pertussis gene sodB, encoding Superoxide dismutase (SOD), was cloned by complementation of an Escherichia coli sodAsodB double mutant. The nucleotide sequence of sodB predicted a 21-kDa protein with homology to manganese- and iron-containing SODs from other organisms. Examination of S...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Gene 1994-05, Vol.142 (1), p.85-89
Hauptverfasser:	DeShazer, David, Barnnan, Jason D., Moran, Michael J., Friedman, Richard L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Base Sequence Biological and medical sciences Bordetella pertussis Bordetella pertussis - enzymology Bordetella pertussis - genetics Cloning, Molecular Electrophoresis, Polyacrylamide Gel Escherichia coli Fundamental and applied biological sciences. Psychology Genes, Bacterial Genes. Genome Genetic Complementation Test homologous recombination human pathogen insertion mutagenesis metalloenzyme Molecular and cellular biology Molecular genetics Molecular Sequence Data Mutagenesis, Insertional Oxidative stress Restriction Mapping Sequence Homology, Amino Acid suicide vector Superoxide Dismutase - genetics Superoxide Dismutase - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	The Bordetella pertussis gene sodB, encoding Superoxide dismutase (SOD), was cloned by complementation of an Escherichia coli sodAsodB double mutant. The nucleotide sequence of sodB predicted a 21-kDa protein with homology to manganese- and iron-containing SODs from other organisms. Examination of SOD activity on gels suggests that B. pertussis extracts have a single SOD containing Fe + as a prosthetic group. A SOD-deβcient mutant was obtained by insertional inactivation of sodB in B. pertussis, confirming that there is only one SOD in this organism.
ISSN:	0378-1119 1879-0038
DOI:	10.1016/0378-1119(94)90359-X