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Cross-linking/mass spectrometry analysis of the AOC complex

ABSTRACT: As a part of a study on how kinetochors are assembled at the centromeres of the chromosomes, cross-linking/mass spectrometry has been applied to investigate interactions between Okp1/ Ame1 heterodimer, which is part of the COMA complex, and CENP-A from Saccharomyces cerevisiae.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Zhuo Chen

LAB HEAD: Juri Rappsilber

PROVIDER: PXD009648 | Pride | 2018-10-30

REPOSITORIES: pride

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Dataset's files

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			Action	DRS
	Rappsilber_CLMS_xlinkAOC-1.raw	Raw
	Rappsilber_CLMS_xlinkAOC-2.raw	Raw
	Rappsilber_CLMS_xlinkAOC-3.raw	Raw
	Rappsilber_CLMS_xlinkAOC_SearchResults.csv	Csv
	recal_Rappsilber_CLMS_xlinkAOC-1.mgf	Mgf

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Publications

The kinetochore module Okp1CENP-Q/Ame1CENP-U is a reader for N-terminal modifications on the centromeric histone Cse4CENP-A.

Anedchenko Ekaterina A EA Samel-Pommerencke Anke A Tran Nguyen Tra My TM Shahnejat-Bushehri Sara S Pöpsel Juliane J Lauster Daniel D Herrmann Andreas A Rappsilber Juri J Cuomo Alessandro A Bonaldi Tiziana T Ehrenhofer-Murray Ann E AE

The EMBO journal 20181102 1

Kinetochores are supramolecular assemblies that link centromeres to microtubules for sister chromatid segregation in mitosis. For this, the inner kinetochore CCAN/Ctf19 complex binds to centromeric chromatin containing the histone variant CENP-A, but whether the interaction of kinetochore components to centromeric nucleosomes is regulated by posttranslational modifications is unknown. Here, we investigated how methylation of arginine 37 (R37Me) and acetylation of lysine 49 (K49Ac) on the CENP-A ...[more]

PMID: 30389668

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