Proteomics

Dataset Information

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Mass spectrometric analysis of proteolytic cleavage related to ArtA and PssA from Haloferax volcanii


ABSTRACT: The S-layer glycoprotein (SLG) of Haloferax volcanii has been shown to be processed and C-terminally linked to a lipid in an archaeosortase A (ArtA)-dependent manner. A C-terminal tripartite structure including a PGF motif is required for the processing of SLG as well as other substrates (Abdul Halim et al., 2013 Mol Microbiol; Abdul Halim et al., 2016 J Bact; Abdul Halim et al., 2017 J Bact; Abdul Halim et al., 2018 Mol Microbiol). In order to gain insights into the mechanism of processing, different cellular fractions (culture supernatant, membrane) from different strains (WT, ArtA KO mutant, ArtA active site mutants, PssA KO mutant) have been analyzed. C-terminal peptides of SLG as well as peptides spanning the PGF motiv were only identified in the mutants lacking processing activity.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Haloferax Volcanii (halobacterium Volcanii)

SUBMITTER: Stefan Schulze  

LAB HEAD: Mechthild Pohlschroder

PROVIDER: PXD011050 | Pride | 2020-05-11

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
Merged_results_GluC.csv Csv
Merged_results_GluC.csv.u.json Csv
Merged_results_trypsin.csv Csv
Merged_results_trypsin.csv.u.json Csv
StS_FASP-RR01_05052017.raw Raw
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Publications


While many aspects of archaeal cell biology remain relatively unexplored, systems biology approaches like mass spectrometry (MS) based proteomics offer an opportunity for rapid advances. Unfortunately, the enormous amount of MS data generated often remains incompletely analyzed due to a lack of sophisticated bioinformatic tools and field-specific biological expertise for data interpretation. Here we present the initiation of the Archaeal Proteome Project (ArcPP), a community-based effort to comp  ...[more]

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