Assigning a function to a conserved archaeal metallo-β-lactamase from Haloferax volcanii

Susan Fischer, Simona John von Freyend, Anice Sabag-Daigle, Charles J. Daniels, Thorsten Allers, Anita Marchfelder

Research output: Contribution to journalArticleResearchpeer-review

6 Citations (Scopus)


The metallo-β-lactamase family of enzymes comprises a large group of proteins with diverse functions in the metabolism of the cell. Among others, this superfamily contains proteins which are involved in DNA and RNA metabolism, acting as nucleases in e. g. repair and maturation. Many proteins have been annotated in prokaryotic genomes as being potential metallo-β-lactamases, but very often the function has not been proven. The protein HVO_2763 from Haloferax volcanii is such a potential metallo-β-lactamase. HVO_2763 has sequence similarity to the metallo-β-lactamase tRNase Z, a tRNA 3′ processing endonuclease. Here, we report the characterisation of this metallo-β-lactamase HVO_2763 in the halophilic archaeon Haloferax volcanii. Using different in vitro assays with the recombinant HVO_2763, we could show that the protein does not have tRNA 3′ processing or exonuclease activity. According to transcriptome analyses of the HVO_2763 deletion strain, expression of proteins involved in membrane transport is downregulated in the mutant. Therefore, HVO_2763 might be involved directly or indirectly in membrane transport.

Original languageEnglish
Pages (from-to)333-343
Number of pages11
Issue number2
Publication statusPublished - Mar 2012
Externally publishedYes


  • Haloferax volcanii
  • HVO_2763
  • Metallo-β-lactamase
  • PhnP
  • tRNase Z

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