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Identification and Functional Analysis of the Gene Cluster for L-arabinose Utilization in Corynebacterium Glutamicum

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Date 2009 Apr 7
PMID 19346355
Citations 18
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Abstract

Corynebacterium glutamicum ATCC 31831 grew on l-arabinose as the sole carbon source at a specific growth rate that was twice that on d-glucose. The gene cluster responsible for l-arabinose utilization comprised a six-cistron transcriptional unit with a total length of 7.8 kb. Three l-arabinose-catabolizing genes, araA (encoding l-arabinose isomerase), araB (l-ribulokinase), and araD (l-ribulose-5-phosphate 4-epimerase), comprised the araBDA operon, upstream of which three other genes, araR (LacI-type transcriptional regulator), araE (l-arabinose transporter), and galM (putative aldose 1-epimerase), were present in the opposite direction. Inactivation of the araA, araB, or araD gene eliminated growth on l-arabinose, and each of the gene products was functionally homologous to its Escherichia coli counterpart. Moreover, compared to the wild-type strain, an araE disruptant exhibited a >80% decrease in the growth rate at a lower concentration of l-arabinose (3.6 g liter(-1)) but not at a higher concentration of l-arabinose (40 g liter(-1)). The expression of the araBDA operon and the araE gene was l-arabinose inducible and negatively regulated by the transcriptional regulator AraR. Disruption of araR eliminated the repression in the absence of l-arabinose. Expression of the regulon was not repressed by d-glucose, and simultaneous utilization of l-arabinose and d-glucose was observed in aerobically growing wild-type and araR deletion mutant cells. The regulatory mechanism of the l-arabinose regulon is, therefore, distinct from the carbon catabolite repression mechanism in other bacteria.

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References
1.
Parche S, Burkovski A, Sprenger G, Weil B, Kramer R, Titgemeyer F . Corynebacterium glutamicum: a dissection of the PTS. J Mol Microbiol Biotechnol. 2001; 3(3):423-8. View

2.
Abramson J, Kaback H, Iwata S . Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: members of the major facilitator superfamily. Curr Opin Struct Biol. 2004; 14(4):413-9. DOI: 10.1016/j.sbi.2004.07.005. View

3.
Kotrbova-Kozak A, Kotrba P, Inui M, Sajdok J, Yukawa H . Transcriptionally regulated adhA gene encodes alcohol dehydrogenase required for ethanol and n-propanol utilization in Corynebacterium glutamicum R. Appl Microbiol Biotechnol. 2007; 76(6):1347-56. DOI: 10.1007/s00253-007-1094-6. View

4.
Kalinowski J, Bathe B, Bartels D, Bischoff N, Bott M, Burkovski A . The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins. J Biotechnol. 2003; 104(1-3):5-25. DOI: 10.1016/s0168-1656(03)00154-8. View

5.
Horazdovsky B, Hogg R . Genetic reconstitution of the high-affinity L-arabinose transport system. J Bacteriol. 1989; 171(6):3053-9. PMC: 210014. DOI: 10.1128/jb.171.6.3053-3059.1989. View