biostudies-literatureAbdul Halim MFNSF | BIO | Division of Molecular and Cellular BiosciencesNational Aeronautics and Space AdministrationU.S. Department of DefenseNIGMS NIH HHS808-15https://www.ebi.ac.uk/biostudies/studies/S-EPMC4810604biostudies-literatureUnknown198(5)<h4>Unlabelled</h4>For years, the S-layer glycoprotein (SLG), the sole component of many archaeal cell walls, was thought to be anchored to the cell surface by a C-terminal transmembrane segment. Recently, however, we demonstrated that the Haloferax volcanii SLG C terminus is removed by an archaeosortase (ArtA), a novel peptidase. SLG, which was previously shown to be lipid modified, contains a C-terminal tripartite structure, including a highly conserved proline-glycine-phenylalanine (PGF) motif. Here, we demonstrate that ArtA does not process an SLG variant where the PGF motif is replaced with a PFG motif (slg(G796F,F797G)). Furthermore, using radiolabeling, we show that SLG lipid modification requires the PGF motif and is ArtA dependent, lending confirmation to the use of a novel C-termJournal of bacteriologyPermuting the PGF Signature Motif Blocks both Archaeosortase-Dependent C-Terminal Cleavage and Prenyl Lipid Attachment for the Haloferax volcanii S-Layer Glycoprotein.PMC4810604NNX10AR84GT32 GM071339MCB-1413158W81XWH-13-1-0426Haft DHKarch KRPohlschroder MAbdul Halim MFGarcia BAZhou YfalsePermuting the PGF Signature Motif Blocks both Archaeosortase-Dependent C-Terminal Cleavage and Prenyl Lipid Attachment for the Haloferax volcanii S-Layer Glycoprotein.<h4>Unlabelled</h4>For years, the S-layer glycoprotein (SLG), the sole component of many archaeal cell walls, was thought to be anchored to the cell surface by a C-terminal transmembrane segment. Recently, however, we demonstrated that the Haloferax volcanii SLG C terminus is removed by an archaeosortase (ArtA), a novel peptidase. SLG, which was previously shown to be lipid modified, contains a C-terminal tripartite structure, including a highly conserved proline-glycine-phenylalanine (PGF) motif. Here, we demonstrate that ArtA does not process an SLG variant where the PGF motif is replaced with a PFG motif (slg(G796F,F797G)). Furthermore, using radiolabeling, we show that SLG lipid modification requires the PGF motif and is ArtA dependent, lending confirmation to the use of a novel C-term2015-01-01T00:00:00Z2015 Dec2026-04-30T07:01:39.92Z2019-03-27T03:10:28ZS-EPMC48106042671293710.1128/JB.00849-1510.1128/jb.00849-15