title: Functional Implications of Domain Organization Within Prokaryotic Rhomboid Proteases.
abstract: Intramembrane proteases are membrane embedded enzymes that cleave transmembrane substrates. This interesting class of enzyme and its water mediated substrate cleavage mechanism occurring within the hydrophobic lipid bilayer has drawn the attention of researchers. Rhomboids are a family of ubiquitous serine intramembrane proteases. Bacterial forms of rhomboid proteases are mainly composed of six transmembrane helices that are preceded by a soluble N-terminal domain. Several crystal structures of the membrane domain of the E. coli rhomboid protease ecGlpG have been solved. Independently, the ecGlpG N-terminal cytoplasmic domain structure was solved using both NMR and protein crystallography. Despite these structures, we still do not know the structure of the full-length protein, nor do we know the functional role of these domains in the cell. This chapter will review the structural and functional roles of the different domains associated with prokaryotic rhomboid proteases. Lastly, we will address questions remaining in the field.
authors.affiliation: Department of Biochemistry, Faculty of Medicine & Dentistry, Membrane Protein Disease Research Group, University of Alberta, Edmonton, AB, Canada. panigrah@ualberta.ca.
authors.forename: Rashmi
authors.initials: R
authors.lastname: Panigrahi
authors.affiliation: Department of Biochemistry, Faculty of Medicine & Dentistry, Membrane Protein Disease Research Group, University of Alberta, Edmonton, AB, Canada. joanne.lemieux@ualberta.ca.
authors.forename: M Joanne
authors.initials: MJ
authors.lastname: Lemieux
mesh_terms: D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000502:physiology; D010450:Endopeptidases / Q000737:chemistry* / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000502:physiology; D008565:Membrane Proteins / Q000737:chemistry* / Q000502:physiology; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D057057:Serine Proteases / Q000737:chemistry* / Q000502:physiology
chemical_list: D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C102898:GlpG protein, E coli; D008565:Membrane Proteins; D010450:Endopeptidases; D057057:Serine Proteases
keywords: Domain organization; Prokaryotic rhomboid proteases; Serine intramembrane proteases