Dataset Information

Characterizing N-Glycosylation of Pilins and Flagellins from Haloferax volcanii

ABSTRACT: Mass spectrometric analysis of cesium chloride purified flagellins and pilins confirmed previously identified N-glycopeptides for FlgA1, revealed additional N-glycopeptides for FlgA1 and FlgA2 and characterized N-glycosylation of PilA1 and PilA2. Analyses were performed using different MS methods (with and withoout applying IS-CID) for samples from wildtype as well as aglB knockout strains.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Haloferax Volcanii (halobacterium Volcanii)

SUBMITTER: Stefan Schulze

LAB HEAD: Mechthild Pohlschroder

PROVIDER: PXD011015 | Pride | 2020-05-11

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Pili_all_results_Hex1.csv	Csv
	Pili_all_results_Hex1HexA1.csv	Csv
	Pili_all_results_Hex1HexA2.csv	Csv
	Pili_all_results_Hex1HexA2MeHexA1.csv	Csv
	Pili_all_results_Hex2HexA2MeHexA1.csv	Csv

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Publications

Identification of Haloferax volcanii Pilin N-Glycans with Diverse Roles in Pilus Biosynthesis, Adhesion, and Microcolony Formation.

Esquivel Rianne N RN Schulze Stefan S Xu Rachel R Hippler Michael M Pohlschroder Mechthild M

The Journal of biological chemistry 20160310 20

N-Glycosylation is a post-translational modification common to all three domains of life. In many archaea, the oligosacharyltransferase (AglB)-dependent N-glycosylation of flagellins is required for flagella assembly. However, whether N-glycosylation is required for the assembly and/or function of the structurally related archaeal type IV pili is unknown. Here, we show that of six Haloferax volcanii adhesion pilins, PilA1 and PilA2, the most abundant pilins in pili of wild-type and ΔaglB strains ...[more]

PMID: 26966177

Publication: 1/2

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