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Journal of Bacteriology, March 2007, p. 1648-1654, Vol. 189, No. 5
0021-9193/07/$08.00+0     doi:10.1128/JB.00841-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Glucosylglycerate Biosynthesis in the Deepest Lineage of the Bacteria: Characterization of the Thermophilic Proteins GpgS and GpgP from Persephonella marina{triangledown}

Joana Costa,1 Nuno Empadinhas,1 and Milton S. da Costa2*

Centro de Neurociências e Biologia Celular, Departamento de Zoologia, Universidade de Coimbra, 3004-517 Coimbra, Portugal,1 Departamento de Bioquímica, Universidade de Coimbra, 3001-401 Coimbra, Portugal2

Received 13 June 2006/ Accepted 7 December 2006

The pathway for the synthesis of glucosylglycerate (GG) in the thermophilic bacterium Persephonella marina is proposed based on the activities of recombinant glucosyl-3-phosphoglycerate (GPG) synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP). The sequences of gpgS and gpgP from the cold-adapted bacterium Methanococcoides burtonii were used to identify the homologues in the genome of P. marina, which were separately cloned and overexpressed as His-tagged proteins in Escherichia coli. The recombinant GpgS protein of P. marina, unlike the homologue from M. burtonii, which was specific for GDP-glucose, catalyzed the synthesis of GPG from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate, with maximal activity at 90°C. The recombinant GpgP protein, like the M. burtonii homologue, dephosphorylated GPG and mannosyl-3-phosphoglycerate (MPG) to GG and mannosylglycerate, respectively, yet at high temperatures the hydrolysis of GPG was more efficient than that of MPG. Gel filtration indicates that GpgS is a dimeric protein, while GpgP is monomeric. This is the first characterization of genes and enzymes for the synthesis of GG in a thermophile.

* Corresponding author. Mailing address: Departamento de Bioquímica, Universidade de Coimbra, 3001-401 Coimbra, Portugal. Phone: 351-239824024. Fax: 351-239826798. E-mail: milton{at}ci.uc.pt.

{triangledown} Published ahead of print on 22 December 2006.

Journal of Bacteriology, March 2007, p. 1648-1654, Vol. 189, No. 5
0021-9193/07/$08.00+0     doi:10.1128/JB.00841-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Alarico, S., da Costa, M. S., Empadinhas, N. (2008). Molecular and Physiological Role of the Trehalose-Hydrolyzing {alpha}-Glucosidase from Thermus thermophilus HB27. J. Bacteriol. 190: 2298-2305 [Abstract] [Full Text]  
  • Fernandes, C., Empadinhas, N., da Costa, M. S. (2007). Single-Step Pathway for Synthesis of Glucosylglycerate in Persephonella marina. J. Bacteriol. 189: 4014-4019 [Abstract] [Full Text]  


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