English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Lipid Anchoring of Archaeosortase Substrates and Midcell Growth in Haloarchaea

Abdul-Halim, M. F., Schulze, S., DiLucido, A., Pfeiffer, F., Bisson Filho, A. W., & Pohlschroder, M. (2020). Lipid Anchoring of Archaeosortase Substrates and Midcell Growth in Haloarchaea. MBIO, 11(2): e00349-20. doi:10.1128/mBio.00349-20.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0006-7323-1 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-7324-0
Genre: Journal Article

Files

show Files
hide Files
:
mBio-2020-Abdul-Halim-e00349-20.full.pdf (Any fulltext), 4MB
Name:
mBio-2020-Abdul-Halim-e00349-20.full.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
open access article
License:
-

Locators

show

Creators

show
hide
 Creators:
Abdul-Halim, Mohd Farid1, Author
Schulze, Stefan1, Author
DiLucido, Anthony1, Author
Pfeiffer, Friedhelm2, Author              
Bisson Filho, Alexandre Wilson1, Author
Pohlschroder, Mechthild1, Author
Affiliations:
1external, ou_persistent22              
2Habermann, Bianca / Computational Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1832284              

Content

show
hide
Free keywords: HALOFERAX-VOLCANII; PROTEIN; GLYCOPROTEIN; ATTACHMENT; BACTERIA; SYNTHASE; FLAFarchaea; Holoferax volcanii; S-layer; archaeosortase; cell division; cell elongation; cell shape; cell surface; haloarchaea; lipid anchoring;
 Abstract: The archaeal cytoplasmic membrane provides an anchor for many surface proteins. Recently, a novel membrane anchoring mechanism involving a peptidase, archaeosortase A (ArtA), and C-terminal lipid attachment of surface proteins was identified in the model archaeon Holoferox volcanii. ArtA is required for optimal cell growth and morphogenesis, and the S-layer glycoprotein (SLG), the sole component of the H. volcanii cell wall, is one of the targets for this anchoring mechanism. However, how exactly ArtA function and regulation control cell growth and morphogenesis is still elusive. Here, we report that archaeal homologs to the bacterial phosphatidylserine synthase (PssA) and phosphatidylserine decarboxylase (PssD) are involved in ArtA-dependent protein maturation. Holoferox volcanii strains lacking either HvPssA or HvPssD exhibited motility, growth, and morphological phenotypes similar to those of an Delta artA mutant. Moreover, we showed a loss of covalent lipid attachment to SLG in the Delta hvpssA mutant and that proteolytic cleavage of the ArtA substrate HVO_0405 was blocked in the Delta hvossA and Delta hvossD mutant strains. Strikingly, ArtA, HvPssA, and HvPssD green fluorescent protein (GFP) fusions colocalized to the midcell position of H. volcanii cells, strongly supporting that they are involved in the same pathway. Finally, we have shown that the SLG is also recruited to the midcell before being secreted and lipid anchored at the cell outer surface. Collectively, our data suggest that haloarchaea use the midcell as the main surface processing hot spot for cell elongation, division, and shape determination. IMPORTANCE The subcellular organization of biochemical processes in space and time is still one of the most mysterious topics in archaeal cell biology. Despite the fact that haloarchaea largely rely on covalent lipid anchoring to coat the cell envelope, little is known about how cells coordinate de novo synthesis and about the insertion of this proteinaceous layer throughout the cell cycle. Here, we report the identification of two novel contributors to ArtA-dependent lipid-mediated protein anchoring to the cell surface, HvPssA and HvPssD. ArtA, HvPssA, and HvPssD, as well as SLG, showed midcell localization during growth and cytokinesis, indicating that haloarchaeal cells confine phospholipid processing in order to promote midcell elongation. Our findings have important implications for the biogenesis of the cell surface.

Details

show
hide
Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000531071300001
DOI: 10.1128/mBio.00349-20
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: MBIO
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: 1752 N ST NW, WASHINGTON, DC 20036-2904 USA : AMER SOC MICROBIOLOGY
Pages: - Volume / Issue: 11 (2) Sequence Number: e00349-20 Start / End Page: - Identifier: ISSN: 2150-7511