Proteomics

Dataset Information

0

Characterizing of Haloferax volcanii Hvo_0405 as a Tat substrate


ABSTRACT: In order to test the hypothesis that Hvo_0405 is a Tat substrate, samples from the membrane and cytoplasm of strains expressing Hvo_0405RR or the mutated Hvo_0405KK were analyzed by mass spectrometry. A semi-enzymatic peptid corresponding to the cleavage of the signal peptide could only be identified in for Hvo_0405RR, indicating that Hvo_0405 is indeed a Tat substrate.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Haloferax Volcanii (halobacterium Volcanii)

SUBMITTER: Stefan Schulze  

LAB HEAD: Mechthild Pohlschroder

PROVIDER: PXD010824 | Pride | 2020-05-11

REPOSITORIES: Pride

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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]

Publication: 1/3

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