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Phosphorylation of Cohesin's Deposition Factor, Scc2 Regulates its Deposition Activity

ABSTRACT: Phosphorylated residues of the budding yeast Scc2 protein were identified using phosphopeptide enrichment and mass spectrometry.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Cell Culture

SUBMITTER: Matthew Wither

LAB HEAD: Paul C. Megee

PROVIDER: PXD001830 | Pride | 2015-09-10

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	Asynchronous_cells_Scc2_band_excision.mzid.gz	Mzid
	Asynchronous_cells_Scc2_band_excision.pride.mztab.gz	Mztab
	Asynchronous_cells_Scc2_band_excision.raw	Raw
	Asynchronous_cells_Scc2_band_excision_ITMSms2cid.mgf	Mgf
	Asynchronous_cells_Scc2_band_excision_ITMSms2cid.pride.mgf.gz	Mgf

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Publications

Phosphorylation of the Scc2 cohesin deposition complex subunit regulates chromosome condensation through cohesin integrity.

Woodman Julie J Hoffman Matthew M Dzieciatkowska Monika M Hansen Kirk C KC Megee Paul C PC

Molecular biology of the cell 20150909 21

The cohesion of replicated sister chromatids promotes chromosome biorientation, gene regulation, DNA repair, and chromosome condensation. Cohesion is mediated by cohesin, which is deposited on chromosomes by a separate conserved loading complex composed of Scc2 and Scc4 in Saccharomyces cerevisiae. Although it is known to be required, the role of Scc2/Scc4 in cohesin deposition remains enigmatic. Scc2 is a phosphoprotein, although the functions of phosphorylation in deposition are unknown. We id ...[more]

PMID: 26354421

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Characterization of R-loop-interacting proteins in embryonic stem cells reveals roles in ribosomal RNA processing and gene expression

Project description:Chromatin-associated RNAs have diverse roles in the nucleus. However, their mechanisms of action are poorly understood, in part due to the inability to identify proteins that specifically associate with chromatin-bound RNAs. Here, we address this problem for a subset of chromatin-associated RNAs that form R-loops—RNA-DNA hybrid structures that include a displaced strand of single-stranded DNA. R-loops generally form co-transcriptionally and have important roles in regulation of gene expression, immunoglobulin class switching, and other processes. However, unresolved R-loops can lead to DNA damage and chromosome instability. To identify factors that may bind and potentially regulate R-loop accumulation or mediate R-loop-dependent functions, we used a comparative immunoprecipitation/mass spectrometry approach, with and without RNA-protein crosslinking, to identify a stringent set of R-loop-binding proteins in mouse embryonic stem cells. We identified 365 R-loop-interacting proteins, which were highly enriched for proteins with predicted RNA-binding functions. We characterized several R-loop-interacting proteins of the DEAD-box family of RNA helicases and found that these proteins localize to the nucleolus and, to a lesser degree, the nucleus. Consistent with their localization patterns, we found that these helicases are required for ribosomal RNA processing and regulation of gene expression. Surprisingly, depletion of these helicases resulted in misregulation of highly overlapping sets of protein-coding genes, including many genes that function in differentiation and development. We conclude that R-loop-interacting DEAD-box helicases have non-redundant roles that are critical for maintaining the normal embryonic stem cell transcriptome.

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2016-02-15 | PXD002372 | Pride

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2016-02-15 | PXD002312 | Pride

Urinary polypeptide ETD/CID analysis, part 2

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