Document Type
Article
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 Link
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: 10.1021/acs.jproteome.7b00530
