Abstract

The degradation of the pentoses d-xylose, l-arabinose and d-ribose in the domain of archaea, in Haloferax volcanii and in Haloarcula and Sulfolobus species, has been shown to proceed via oxidative pathways to generate α-ketoglutarate. Here, we report that the haloarchaeal Halorhabdus species utilize the bacterial-type non-oxidative degradation pathways for pentoses generating xylulose-5-phosphate. The genes of these pathways are each clustered and were constitutively expressed. Selected enzymes involved in d-xylose degradation, xylose isomerase and xylulokinase, and those involved in l-arabinose degradation, arabinose isomerase and ribulokinase, were characterized. Further, d-ribose degradation in Halorhabdus species involves ribokinase, ribose-5-phosphate isomerase and d-ribulose-5-phosphate-3-epimerase. Ribokinase of Halorhabdus tiamatea and ribose-5-phosphate isomerase of Halorhabdus utahensis were characterized. This is the first report of pentose degradation via the bacterial-type pathways in archaea, in Halorhabdus species that likely acquired these pathways from bacteria. The utilization of bacterial-type pathways of pentose degradation rather than the archaeal oxidative pathways generating α-ketoglutarate might be explained by an incomplete gluconeogenesis in Halorhabdus species preventing the utilization of α-ketoglutarate in the anabolism.

Highlights

  • The pentoses d-xylose, l-arabinose and d-ribose are abundant in nature being part of hemicellulose material of plants and as component of ribonucleotides

  • Genome analyses indicate that Halorhabdus utahensis unlike other haloarchaea contains genes encoding putative enzymes of the classical pathways of d-xylose and l-arabinose degradation reported for most bacteria (Anderson et al 2011)

  • D-ribose degradation in H. utahensis and Halorhabdus tiamatea and the enzymes involved were studied revealing the operation of the bacterial-type pathway of D-ribose degradation

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Summary

Introduction

The pentoses d-xylose, l-arabinose and d-ribose are abundant in nature being part of hemicellulose material of plants and as component of ribonucleotides. We report transcription of selected genes of d-xylose and l-arabinose degradation in H. utahensis and the characterization of their encoded enzymes. We found that d-ribose is degraded in H. utahensis and Halorhabdus tiamatea to xylulose-5-phosphate by the bacterial pathway involving the enzymes ribokinase, ribose-5-phosphate isomerase and d-ribulose-5-phosphate3-epimerase.

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