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    STUDIA BIOLOGIA - Issue no. 1 / 2019  
         
  Article:   C-TERMINAL LIPID-ANCHORING OF HALOFERAX VOLCANII SURFACE PROTEINS.

Authors:  MECHTHILD POHLSCHRÖDER, ANTHONY DILUCIDO , FRIEDHELM PFEIFFER, F. MOHD ABDUL HALIM. 		 
       
         
  Abstract:  The microbial cell surface proteins play various critical roles such as mediating the intercellular communications, nutrient uptake, surface adhesion, motility and providing cell shape. Many surface proteins are anchored via insertion of a transmembrane (TM) domain in the cytoplasmic membrane or are covalently-linked with a lipid moiety to N-terminally anchor it to the membrane. Recently, a novel anchoring mechanism in which the proteins are C-terminally processed, and covalently-lipid anchored at its C-terminus via an enzyme known as archaeosortase (ArtA) has been identified. Target proteins that are recognized and processed by ArtA carry a distinct C-terminal tripartite structure consisting of a conserved PGF motif, followed by a hydrophobic domain and positively charged residues. Molecular biological, biochemical and microscopic analyses of the model archaeon Haloferax volcanii confirmed the importance of the conserved PGF domain for ArtA-dependent processing, identified ArtA-dependent processing of diverse Tat as well as Sec substrates, including the S-layer glycoprotein, and revealed the active site of the ArtA peptidase. Moreover, two enzymes involved in archaetidylethanolamine biosynthesis are critical for processing and lipid anchoring of ArtA substrates. Since archaeosortases, and their bacterial homologs, the exosortases, which to date have only been studied in silico, are found in a broad array of archaea and bacteria, our findings have important implications for cell surface biogenesis in a wide variety of prokaryotes.

Keywords: archaeosortase, cell shape, cell surface anchoring, motility, S-layer glycoprotein. 		 
         
     
         
         
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