PXD018353 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Altered N-glycan composition impacts flagella mediated adhesion in Chlamydomonas reinhardtii |
Description | For the unicellular alga Chlamydomonas reinhardtii, the presence of N-glycosylated proteins on the surface of two flagella is crucial for both cell-cell interaction during mating and flagellar surface adhesion. However, it is not known whether only the presence or also the composition of N-glycans attached to respective proteins is important for these processes. To this end, we tested several C. reinhardtii insertional mutants and a CRIPSR/Cas9 knockout mutant of xylosyltransferase 1A, all possessing altered N-glycan compositions. Taking advantage of atomic force microscopy and micropipette force measurements, our data revealed that reduction in N-glycan complexity impedes the adhesion force required for binding the flagella to surfaces as demonstrated by force spectroscopy and impairs polystyrene bead binding and transport. Notably, assembly, Intraflagellar Transport and FMG-1B transport into flagella are not affected by altered N-glycosylation. Thus, we conclude that proper N-glycosylation of flagellar proteins is crucial for adhering C. reinhardtii cells onto surfaces, indicating that N-glycans mediate surface adhesion via direct surface contact. Data deposited here include IS-CID data verifying altered N-glycan patterns in flagella of mutants analysed (Ursgal-SugarPy-flagella-IM-results.xls) as well as the N-glycoproteomic characterization of the novel CRISPRXylT1A mutant (Ursgal-SugarPy-CIRSPR-mutant-results.xls). Regarding the latter, PRM measurements verifying the knock out of XylT1A are also deposited here (Results_PRM-measurement_quantification_GT.xls). Further, label free quantification data on isolated flagella of original IM strains verifying that altered N-glycosylation does not impact flagellar protein localization can be found within this dataset (Flagella_IM-WT_ normalized_5_proteins.pdResult). |
HostingRepository | PRIDE |
AnnounceDate | 2020-12-22 |
AnnouncementXML | Submission_2020-12-22_11:02:51.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Lara Hoepfner |
SpeciesList | scientific name: Chlamydomonas reinhardtii; NCBI TaxID: 3055; |
ModificationList | No PTMs are included in the dataset |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-04-03 07:38:52 | ID requested | |
⏵ 1 | 2020-12-22 11:02:51 | announced | |
2 | 2024-10-22 05:17:02 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Chlamydomonas reinhardtii, N-glycosylation, Flagella, Adhesion, LC-MS/MS, SugarPy, PRM |
Contact List
Michael Hippler |
contact affiliation | Institute for Plant Biology and Biotechnology, University of Münster, Germany |
contact email | mhippler@uni-muenster.de |
lab head | |
Lara Hoepfner |
contact affiliation | IBBP-Plant Biochemistry and Biotechnology AG Prof. Dr. Michael Hippler University of Münster |
contact email | l_hoep03@wwu.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD018353
- Label: PRIDE project
- Name: Altered N-glycan composition impacts flagella mediated adhesion in Chlamydomonas reinhardtii