Abstract
Rhomboids are conserved intramembrane serine proteases involved in cell signaling processes. Their role in prokaryotes is scarcely known and remains to be investigated in Archaea. We previously constructed a rhomboid homologue deletion mutant (?rhoII) in Haloferax volcanii, which showed reduced motility, increased novobiocin sensitivity, and an N- glycosylation defect. To address the impact of rhoII deletion on H. volcanii physiology, the proteomes of mutant and parental strains were compared by shotgun proteomics. A total of 1847 proteins were identified (45.8% of H. volcanii predicted proteome), from which 103 differed in amount. Additionally, the mutant strain evidenced 99 proteins with altered electrophoretic migration, which suggested differential post-translational processing/modification. Integral membrane proteins that evidenced variations in concentration, electrophoretic migration, or semitryptic cleavage in the mutant were considered as potential RhoII targets. These included a PrsW protease homologue (which was less stable in the mutant strain), a predicted halocyanin, and six integral membrane proteins potentially related to the mutant glycosylation (S-layer glycoprotein, Agl15) and cell adhesion/motility (flagellin1, HVO_1153, PilA1, and PibD) defects. This study investigated for the first time the impact of a rhomboid protease on the whole proteome of an organism.
DOI
10.1021/acs.jproteome.7b00530
Publication Date
2018-03-02
Publication Title
Journal of Proteome Research
Volume
17
Issue
3
Publisher
American Chemical Society
ISSN
1535-3907
Embargo Period
2024-11-19
First Page
961
Last Page
977
Recommended Citation
Costa, M., Cerletti, M., Paggi, R., Trötschel, C., & et al. (2018) 'Haloferax volcanii Proteome Response to Deletion of a Rhomboid Protease Gene', Journal of Proteome Research, 17(3), pp. 961-977. American Chemical Society: Available at: https://doi.org/10.1021/acs.jproteome.7b00530
