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Crosslinking/mass spectrometry (CLMS) analysis of Cohesin complex

ABSTRACT: The ring-shaped cohesin complex is thought to fulfil its roles in sister chromatid cohesion, genome stability and gene regulation by topologically encircling DNAs. The ring is formed by two Structural Maintenance of Chromosome (SMC) subunits, whose ATPase heads are linked by a kleisin subunit. Additional components, including the Mis4Scc2/NIPL cohesin loader, engage the kleisin. We applied crosslinking mass spectrometry to characterize cohesion complex in two conditions: initial binding and gripping state.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Schizosaccharomyces Pombe 972h-

SUBMITTER: Zhuo Chen

LAB HEAD: Juri Rappsilber

PROVIDER: PXD018608 | Pride | 2020-08-04

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	Pombe_CohesinComplex_Rappsilber.fasta	Fasta
	SDAxCohesin_GrippingState_PSMmatches_Rappsilber.csv	Csv
	SDAxCohesin_GrippingState_SECf10-R1_Rappsilber.raw	Raw
	SDAxCohesin_GrippingState_SECf10-R2_Rappsilber.raw	Raw
	SDAxCohesin_GrippingState_SECf5-R1_Rappsilber.raw	Raw

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