Histidine Degradation via an Aminotransferase Increases the Nutritional Flexibility of Candida glabrata

Author:

Brunke Sascha12,Seider Katja1,Richter Martin Ernst23,Bremer-Streck Sibylle3,Ramachandra Shruthi4,Kiehntopf Michael23,Brock Matthias45,Hube Bernhard125

Affiliation:

1. Department of Microbial Pathogenicity Mechanisms, Hans Knoell Institute, Jena, Germany

2. Center for Sepsis Control and Care (CSCC), Jena University Hospital, Jena, Germany

3. Institute for Clinical Chemistry and Laboratory Medicine, Jena University Hospital, Jena, Germany

4. Research Group Microbial Biochemistry and Physiology, Hans Knoell Institute, Jena, Germany

5. Friedrich Schiller University, Jena, Germany

Abstract

ABSTRACT The ability to acquire nutrients during infections is an important attribute in microbial pathogenesis. Amino acids are a valuable source of nitrogen if they can be degraded by the infecting organism. In this work, we analyzed histidine utilization in the fungal pathogen of humans Candida glabrata . Hemiascomycete fungi, like C. glabrata or Saccharomyces cerevisiae , possess no gene coding for a histidine ammonia-lyase, which catalyzes the first step of a major histidine degradation pathway in most other organisms. We show that C. glabrata instead initializes histidine degradation via the aromatic amino acid aminotransferase Aro8. Although ARO8 is also present in S. cerevisiae and is induced by extracellular histidine, the yeast cannot use histidine as its sole nitrogen source, possibly due to growth inhibition by a downstream degradation product. Furthermore, C. glabrata relies only on Aro8 for phenylalanine and tryptophan utilization, since ARO8 , but not its homologue ARO9 , was transcriptionally activated in the presence of these amino acids. Accordingly, an ARO9 deletion had no effect on growth with aromatic amino acids. In contrast, in S. cerevisiae , ARO9 is strongly induced by tryptophan and is known to support growth on aromatic amino acids. Differences in the genomic structure of the ARO9 gene between C. glabrata and S. cerevisiae indicate a possible disruption in the regulatory upstream region. Thus, we show that, in contrast to S. cerevisiae , C. glabrata has adapted to use histidine as a sole source of nitrogen and that the aromatic amino acid aminotransferase Aro8, but not Aro9, is the enzyme required for this process.

Publisher

American Society for Microbiology

Subject

Molecular Biology,General Medicine,Microbiology

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