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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/6165

Título: Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis
Autor: Godinho, Lia M.
Sá-Nogueira, Isabel de
Palavras-chave: Gene regulation
AraL
Bacillus subtilis
HAD superfamily (IIA)
Sugar phosphatase
Issue Date: 2011
Editora: Wiley-Blackwell
Citação: FEBS Journal 278 (2011) 2511–2524
Resumo: AraL from Bacillus subtilis is a member of the ubiquitous haloalkanoate dehalogenase superfamily. The araL gene has been cloned, over-expressed in Escherichia coli and its product purified to homogeneity. The enzyme displays phosphatase activity, which is optimal at neutral pH (7.0) and 65 C. Substrate screening and kinetic analysis showed AraL to have low specificity and catalytic activity towards several sugar phosphates, which are metabolic intermediates of the glycolytic and pentose phosphate pathways. On the basis of substrate specificity and gene context within the arabinose metabolic operon, a putative physiological role of AraL in the detoxification of accidental accumulation of phosphorylated metabolites has been proposed. The ability of AraL to catabolize several related secondary metabolites requires regulation at the genetic level. In the present study, using site-directed mutagenesis, we show that the production of AraL is regulated by a structure in the translation initiation region of the mRNA, which most probably blocks access to the ribosome-binding site, preventing protein synthesis. Members of haloalkanoate dehalogenase subfamily IIA and IIB are characterized by a broad-range and overlapping specificity anticipating the need for regulation at the genetic level. We provide evidence for the existence of a genetic regulatory mechanism controlling the production of AraL.
Descrição: FEBS journal, Volume 278, Issue 14, pages 2511-2524, July 2011
URI: http://hdl.handle.net/10362/6165
ISSN: 1742-4658
Appears in Collections:FCT: DCV - Artigos em revista internacional com arbitragem científica

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