منابع مشابه
Regulation of Brucella abortus catalase.
All aerobic organisms have mechanisms that protect against oxidative compounds. Catalase, peroxidase, superoxide dismutase, glutathione, and thioredoxin are widely distributed in many taxa and constitute elements of a nearly ubiquitous antioxidant metabolic strategy. Interestingly, the regulatory mechanisms that control these elements are rather different depending on the nature of the oxidativ...
متن کاملRegulation of Brucella abortus catalase as a defensive mechanism against oxidative stress
In this study, we investigate the expression of Brucella abortus proteins in resporise to oxidative stress. The focus is on several proteins thought to be involved in bacterial protection. We show that catalase and Cu-Zn superoxide dismutase are regulated in response to H2O2 or by superoxide, whereas expression of Hsp70 and Hsp60 are not dramatically affected by oxidative stress. The regulation...
متن کاملBrucella abortus endocarditis.
T HE purpose of this report is to describe the successful treatment of a case of bacterial endocarditis due to Brucella abortus. As far as I have been able to discover at the date of writing, no successfully treated case of this disease has been reported previously, with the exception of a case of mixed bacterial endocarditis presented in 1954 by Quinn and Brown.' A second case of treated Br. a...
متن کاملIdentification of Brucella abortus OxyR and its role in control of catalase expression.
We report the cloning and sequencing of the Brucella abortus oxyR homolog and provide evidence that the transcription product of this gene binds to the B. abortus catalase promoter region. A gene replacement/deletion Brucella oxyR mutant exhibits increased sensitivity to prolonged exposure to H(2)O(2) and is unable to adapt to H(2)O(2) in the environment.
متن کاملBrucella abortus catalase is a periplasmic protein lacking a standard signal sequence.
A periplasmic catalase has been purified and cloned from Brucella abortus. The functional enzyme is a tetramer with a subunit molecular weight of 55,000. All evidence indicates that a typical N-terminal signal sequence is not associated with the export of this protein to the periplasm.
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 2000
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.68.7.3861-3866.2000