Dataset Information

Tandem affinity purification of histones, coupled to mass spectrometry, identifies new sites of post-translational modification and associated proteins in Saccharomyces cerevisiae

ABSTRACT: Our results can be considered as a starting point to gain understanding of how nucleosome modification and composition affect basic cellular processes in yeast.

INSTRUMENT(S): TripleTOF 5600

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

SUBMITTER: Luz Valero

LAB HEAD: Mercè Pamblanco

PROVIDER: PXD002671 | Pride | 2016-01-28

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	H3bufferA_F002142.mgf	Mgf
	H3bufferA_F002142.mzid.gz	Mzid
	H3bufferA_F002142.pride.mgf.gz	Mgf
	H3bufferA_F002142.pride.mztab.gz	Mztab
	H3bufferW_F002146.mgf	Mgf

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Publications

Tandem affinity purification of histones, coupled to mass spectrometry, identifies associated proteins and new sites of post-translational modification in Saccharomyces cerevisiae.

Valero M Luz ML Sendra Ramon R Pamblanco Mercè M

Journal of proteomics 20160109

Histones and their post-translational modifications contribute to regulating fundamental biological processes in all eukaryotic cells. We have applied a conventional tandem affinity purification strategy to histones H3 and H4 of the yeast Saccharomyces cerevisiae. Mass spectrometry analysis of the co-purified proteins revealed multiple associated proteins, including core histones, which indicates that tagged histones may be incorporated to the nucleosome particle. Among the many other co-isolate ...[more]

PMID: 26778144

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