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Structural analyses of the deduced amino acid sequences of a novel type heme–copper terminal oxidase, cytochrome aco3, from alkalophilic Bacillus YN-2000

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Abstract:

Cytochrome aco3 from a facultatively alkalophilic bacterium, Bacillus YN-2000, was found to be alkaline- and heat-tolerant. To better understand the structural features of Bacillus YN-2000 cytochrome aco3, the gene encoding this enzyme was cloned and sequenced. Nucleotide sequence analyses of the region neighboring the acoI (subunit I) gene revealed that the acoII (subunit II) and acoIII (subunit III) genes were concomitantly clustered upstream and downstream of the acoI gene, respectively, forming an operon with transcriptional polarity. The deduced amino acid sequence of subunit I was highly similar to that of cytochrome caa3 from thermophilic bacterium Bacillus PS3 in which the heme a3 could be replaced with heme o. Furthermore, a marked paucity of basic amino acid residues was found in the cytochrome c-binding subunit II, which might be a result of the adaptation to a highly alkaline external milieu.Key words: cytochrome c oxidase, alkalophile, thermostability, heme o, Bacilli.

Le cytochrome aco3 du Bacillus YN-2000, une bactérie alcalophile facultative, s'est révélé tolérant à la température et aux conditions alcalines. Pour mieux connaître la structure du cytochrome aco3 du Bacillus YN-2000, le gène qui code cette enzyme a été cloné et séquencé. Les analyses de la séquence des nucléotides de la région avoisinante du gène acoI (sous-unité I) ont révélé que les gènes acoII (sous-unité II) et acoIII (sous-unité III) étaient regroupés de façon concominante respectivement en amont et en aval du gène acoI, formant un opéron ayant une polarité de transcription. La séquence des acides aminés obtenue pour la sous-unité I était très semblable à celle du cytochrome caa3 de la bactérie thermophile de Bacillus PS3, dans laquelle l'hème a3 peut être remplacé par l'hème o. De plus des résidus d'acides aminés basiques ont rarement été retrouvés dans la sous-unité II de liaison au cytochrome c, ce qui pourrait être le résultat d'une adaptation à un milieu externe fortement alcalin.Mots clés : cytochrome c oxydase, alcalophile, thermostabilité, hème o, Bacilli.[Traduit par la Rédaction]

Keywords: Bacilli; alcalophile; alkalophile; cytochrome c oxidase; cytochrome c oxydase; heme o; hème o; thermostability; thermostabilité

Document Type: Research Article

Publication date: December 1, 2001

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  • Published since 1954, this monthly journal contains new research in the field of microbiology including applied microbiology and biotechnology; microbial structure and function; fungi and other eucaryotic protists; infection and immunity; microbial ecology; physiology, metabolism and enzymology; and virology, genetics, and molecular biology. It also publishes review articles and notes on an occasional basis, contributed by recognized scientists worldwide.
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