1. Haloferax volcanii Proteome Response to Deletion of a Rhomboid Protease Gene
- Author
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Ansgar Poetsch, Maria Ines Gimenez, Roberto A. Paggi, Rosana Esther de Castro, Christian Trötschel, Micaela Cerletti, and Mariana Inés Costa
- Subjects
0301 basic medicine ,Proteases ,Spectrometry, Mass, Electrospray Ionization ,Glycosylation ,Protease substrate ,Proteome ,medicine.medical_treatment ,Archaeal Proteins ,Mutant ,Biochemistry ,Substrate Specificity ,Ciencias Biológicas ,03 medical and health sciences ,chemistry.chemical_compound ,Biología Celular, Microbiología ,Endopeptidases ,Metalloproteins ,medicine ,Shotgun proteomics ,Cell Adhesion ,Integral membrane protein ,Rhomboid protease ,Haloferax volcanii ,Protease ,030102 biochemistry & molecular biology ,biology ,Chemistry ,Halorerax volcanii ,Membrane Proteins ,Molecular Sequence Annotation ,General Chemistry ,biology.organism_classification ,Archea ,Cell biology ,DNA-Binding Proteins ,030104 developmental biology ,Gene Ontology ,Gene Expression Regulation, Archaeal ,Protein Processing, Post-Translational ,CIENCIAS NATURALES Y EXACTAS ,Gene Deletion ,Bacterial Outer Membrane Proteins - 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 (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, 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. Fil: Costa, Mariana Inés. Universidad Nacional de Mar del Plata; Argentina Fil: Cerletti, Micaela. Universidad Nacional de Mar del Plata; Argentina Fil: Paggi, Roberto Alejandro. Universidad Nacional de Mar del Plata; Argentina Fil: Trötschel, Christian. Ruhr Universität Bochum; Alemania Fil: de Castro, Rosana Esther. Universidad Nacional de Mar del Plata; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina Fil: Poetsch, Ansgar. Ruhr Universität Bochum; Alemania Fil: Gimenez, Maria Ines. Universidad Nacional de Mar del Plata; Argentina
- Published
- 2018