In:
PLOS Biology, Public Library of Science (PLoS), Vol. 19, No. 6 ( 2021-6-17), p. e3001277-
Abstract:
Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are largely missing in prokaryotes. Here, we extend the phenotypic characterization of N -glycosylation pathway mutants in Haloferax volcanii and provide a detailed glycoproteome for this model archaeon through the mass spectrometric analysis of intact glycopeptides. Using in-depth glycoproteomic datasets generated for the wild-type (WT) and mutant strains as well as a reanalysis of datasets within the Archaeal Proteome Project (ArcPP), we identify the largest archaeal glycoproteome described so far. We further show that different N -glycosylation pathways can modify the same glycosites under the same culture conditions. The extent and complexity of the Hfx . volcanii N -glycoproteome revealed here provide new insights into the roles of N -glycosylation in archaeal cell biology.
Type of Medium:
Online Resource
ISSN:
1545-7885
DOI:
10.1371/journal.pbio.3001277
DOI:
10.1371/journal.pbio.3001277.g001
DOI:
10.1371/journal.pbio.3001277.g002
DOI:
10.1371/journal.pbio.3001277.g003
DOI:
10.1371/journal.pbio.3001277.g004
DOI:
10.1371/journal.pbio.3001277.g005
DOI:
10.1371/journal.pbio.3001277.t001
DOI:
10.1371/journal.pbio.3001277.t002
DOI:
10.1371/journal.pbio.3001277.t003
DOI:
10.1371/journal.pbio.3001277.t004
DOI:
10.1371/journal.pbio.3001277.s001
DOI:
10.1371/journal.pbio.3001277.s002
DOI:
10.1371/journal.pbio.3001277.s003
DOI:
10.1371/journal.pbio.3001277.s004
DOI:
10.1371/journal.pbio.3001277.s005
DOI:
10.1371/journal.pbio.3001277.s006
DOI:
10.1371/journal.pbio.3001277.s007
DOI:
10.1371/journal.pbio.3001277.s008
DOI:
10.1371/journal.pbio.3001277.s009
DOI:
10.1371/journal.pbio.3001277.s010
DOI:
10.1371/journal.pbio.3001277.s011
DOI:
10.1371/journal.pbio.3001277.r001
DOI:
10.1371/journal.pbio.3001277.r002
DOI:
10.1371/journal.pbio.3001277.r003
DOI:
10.1371/journal.pbio.3001277.r004
DOI:
10.1371/journal.pbio.3001277.r005
DOI:
10.1371/journal.pbio.3001277.r006
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2021
detail.hit.zdb_id:
2126773-X
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