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Title 

Molecular cloning and functional characterization of the genes encoding benzoate and p-hydroxybenzoate degradation by the halophilic Chromohalobacter sp. strain HS-2

Authors 

D KimS W KimK Y ChoiJong Suk LeeE Kim

Publisher 

Wiley-Blackwell

Issue Date 

2008

Citation 

FEMS Microbiology Letters, vol. 280, no. 2, pp. 235-241

Keywords 

benzoatechromohalobacterhalophileP-hydroxybenzoate4 hydroxybenzoate hydroxylasebenzoate 1,2 dioxygenasebenzoate dihydrodiolcatechol 1,2 dioxygenaseprotocatechuate 3,4 dioxygenaseprotocatechuic acid

Abstract 

Chromohalobacter sp. strain HS-2 was isolated from salted fermented clams and analyzed for the ability to grow on benzoate and p-hydroxybenzoate as the sole carbon and energy source. HS-2 was characterized as moderately halophilic, with an optimal NaCl concentration of 10%. The genes encoding the benzoate metabolism were cloned into a cosmid vector, sequenced, and then analyzed to reveal the benzoate (benABCD) and catechol (catBCA) catabolic genes, both of which are flanked on either side by LysR-type transcriptional regulator (catR) and membrane transport protein for benzoate (benE) in the gene order catRBCAbenABCDE. Near the large cat-ben cluster, a p-hydroxybenzoate hydroxylase gene (pobA) and two putative regulatory genes (pcaQ and pobR) were additionally detected. The HS-2 genes involved in benzoate and p-hydroxybenzoate degradation are tightly clustered within a c. 19 kb region, and show quite a different genetic organization from those of other benzoate catabolic genes. Reverse transcriptase-PCR experiments show that benzoate induces the expression of benzoate 1,2-dioxygenase, catechol 1,2-dioxygenase, and protocatechuate 3,4-dioxygenase while p-hydroxybenzoate only induced the expression of p-hydroxybenzoate hydroxylase. When expressed in Escherichia coli, benzoate 1,2-dioxygenase (BenABC) and p-hydroxybenzoate hydroxylase (PobA) transformed benzoate and p-hydroxybenzoate into cis-benzoate dihydrodiol and protocatechuate, respectively.

ISSN 

0378-1097

Link 

http://dx.doi.org/10.1111/j.1574-6968.2008.01067.x

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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