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  Haloferax volcanii archaeosortase is required for motility, mating, and C-terminal processing of the S-layer glycoprotein

Abdul Halim, M. F., Pfeiffer, F., Zou, J., Frisch, A., Haft, D., Wu, S., et al. (2013). Haloferax volcanii archaeosortase is required for motility, mating, and C-terminal processing of the S-layer glycoprotein. MOLECULAR MICROBIOLOGY, 88(6), 1164-1175. doi:10.1111/mmi.12248.

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 Creators:
Abdul Halim, Mohd Farid1, Author
Pfeiffer, Friedhelm2, Author           
Zou, James1, Author
Frisch, Andrew1, Author
Haft, Daniel1, Author
Wu, Si1, Author
Tolic, Nikola1, Author
Brewer, Heather1, Author
Payne, Samuel H.1, Author
Pasa-Tolic, Ljiljana1, Author
Pohlschroder, Mechthild1, Author
Affiliations:
1external, ou_persistent22              
2Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565164              

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Free keywords: GRAM-POSITIVE BACTERIA; SURFACE-PROTEINS; STAPHYLOCOCCUS-AUREUS; CELL-WALL; PROTEOMIC ANALYSES; ACCURATE MASS; TAG STRATEGY; SORTASE; SYSTEM; ATTACHMENT
 Abstract: Cell surfaces are decorated by a variety of proteins that facilitate interactions with their environments and support cell stability. These secreted proteins are anchored to the cell by mechanisms that are diverse, and, in archaea, poorly understood. Recently published in silico data suggest that in some species a subset of secreted euryarchaeal proteins, which includes the S-layer glycoprotein, is processed and covalently linked to the cell membrane by enzymes referred to as archaeosortases. In silico work led to the proposal that an independent, sortase-like system for proteolysis-coupled, carboxy-terminal lipid modification exists in bacteria (exosortase) and archaea (archaeosortase). Here, we provide the first in vivo characterization of an archaeosortase in the haloarchaeal model organism Haloferax volcanii. Deletion of the artA gene (HVO_0915) resulted in multiple biological phenotypes: (a) poor growth, especially under low-salt conditions, (b) alterations in cell shape and the S-layer, (c) impaired motility, suppressors of which still exhibit poor growth, and (d) impaired conjugation. We studied one of the ArtA substrates, the S-layer glycoprotein, using detailed proteomic analysis. While the carboxy-terminal region of S-layer glycoproteins, consisting of a putative threonine-rich O-glycosylated region followed by a hydrophobic transmembrane helix, has been notoriously resistant to any proteomic peptide identification, we were able to identify two overlapping peptides from the transmembrane domain present in the artA strain but not in the wild-type strain. This clearly shows that ArtA is involved in carboxy-terminal post-translational processing of the S-layer glycoprotein. As it is known from previous studies that a lipid is covalently attached to the carboxy-terminal region of the S-layer glycoprotein, our data strongly support the conclusion that archaeosortase functions analogously to sortase, mediating proteolysis-coupled, covalent cell surface attachment.

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Language(s): eng - English
 Dates: 2013-06
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000320174300011
DOI: 10.1111/mmi.12248
 Degree: -

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Title: MOLECULAR MICROBIOLOGY
Source Genre: Journal
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Publ. Info: 111 RIVER ST, HOBOKEN 07030-5774, NJ USA : WILEY-BLACKWELL
Pages: - Volume / Issue: 88 (6) Sequence Number: - Start / End Page: 1164 - 1175 Identifier: ISSN: 0950-382X