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Hydrophobic carboxy-terminal residues dramatically reduce protein levels in the haloarchaeon Haloferax volcanii

University of Florida

Proteolysis is important not only to cell physiology but also to the successful development of biocatalysts. While a wide-variety of signals are known to trigger protein degradation in bacteria and eukaryotes, these mechanisms are poorly understood in archaea known for their ability to withstand harsh conditions. Here we present a systematic study in which single C-terminal amino acid residues were added to a reporter protein and shown to influence its levels in an archaeal cell. All twenty amino acid residues were examined for their impact on protein levels, using the reporter protein soluble modified red-shifted green fluorescent protein (smRS-GFP) expressed in the haloarchaeon Haloferax volcanii as a model system. Our results demonstrate that addition of hydrophobic residues including Leu, Cys, Met, Phe, Ala, Tyr, Ile and Val had the most pronounced reduction in smRS-GFP levels compared to the addition of either neutral or charged hydrophilic residues. In contrast to the altered protein levels, the C-terminal alterations had no influence on smRS-GFP-specific transcript levels, thus revealing the effect is post-transcriptional.

¹ E-mail: jmaupin{at}ufl.edu