Haloferax volcanii Proteome Response to Deletion of a Rhomboid Protease Gene.

MARIANA I. COSTA; CHRISTIAN TROETSCHEL; MARÍA I. GIMÉNEZ; MICAELA CERLETTI; ROSANA E. DE CASTRO; ROBERTO A. PAGGI; ANSGAR POETSCH

JOURNAL OF PROTEOME RESEARCH

AMER CHEMICAL SOC

Lugar: Washington; Año: 2018 vol. 17 p. 961 - 977

1535-3893

AbstractRhomboids 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 homolog deletion mutant (ΔrhoII) 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, suggesting differential post-translational processing/modification. Integral membrane proteins that evidenced variations in concentration and/or electrophoretic migration in the mutant were considered as potential RhoII targets. These included a PrsW protease homolog (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 any organism.