Proteomics

Dataset Information

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Cross-linking of the microtubule binding N-terminal domain of the companion of cellulose synthase 1 protein (CC1∆C223) from Arabidopsis thaliana with tubulin

ABSTRACT: In this study, we use Cross-linking Mass Spectrometry to identify the interaction sites of the microtubule binding N-terminal domain of the companion of cellulose synthase 1 protein (CC1∆C223) from Arabidopsis thaliana with tubulin. We consistently detected four cross-linked peptides of CC1∆C223 to β-tubulin (K40 to E111, K94 to E111, K96 to E111 and K96 to E158; letters and numbers indicate specific amino acids in the protein sequence of CC1∆C223 and β-tubulin, respectively) and one cross-linked peptide of CC1∆C223 to α-tubulin (K40 to D327).

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Christopher Kesten  

LAB HEAD: Staffan Persson

PROVIDER: PXD009260 | Pride | 2019-01-08

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
CruxCandidatesassignedIons.xlsx Xlsx
CruxResultscombined.xlsx Xlsx
Ingel1.mgf Mgf
Ingel1.mzML Mzml
Ingel1.raw Raw
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Publications

Microtubules are filamentous structures necessary for cell division, motility and morphology, with dynamics critically regulated by microtubule-associated proteins (MAPs). Here we outline the molecular mechanism by which the MAP, COMPANION OF CELLULOSE SYNTHASE1 (CC1), controls microtubule bundling and dynamics to sustain plant growth under salt stress. CC1 contains an intrinsically disordered N-terminus that links microtubules at evenly distributed points through four conserved hydrophobic regi  ...[more]

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