Dataset Information

The histone methyltransferase SETD2 couples transcription and splicing by engaging pre-mRNA processing factors through its SHI domain

ABSTRACT: The domains of SETD2, a known histone methyltransferase were investigated for specific interaction partners and function using a number of biochemical assays and affinity purification mass spectrometry. The C-terminal domain, named SETD2C, was identified to interact with hnRNP-L through a previously uncharacterized domain. These findings demonstrate the crosstalk between the transcription and splicing machinery.

INSTRUMENT(S): LTQ Orbitrap, LTQ

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Michaella Levy

LAB HEAD: Laurence Florens

PROVIDER: PXD019538 | Pride | 2021-02-01

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Hs_Halo-CC1a_293T-WCE_Halo-AP-1_rKCTi_L5_10.mzid.gz	Mzid
	Hs_Halo-CC1a_293T-WCE_Halo-AP-1_rKCTi_L5_101.RAW	Raw
	Hs_Halo-CC1a_293T-WCE_Halo-AP-1_rKCTi_L5_101.mgf	Mgf
	Hs_Halo-CC1a_293T-WCE_Halo-AP-1_rKCTi_L5_101.ms2	Other
	Hs_Halo-CC1a_293T-WCE_Halo-AP-1_rKCTi_L5_101.sqt	Other

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Publications

The methyltransferase SETD2 couples transcription and splicing by engaging mRNA processing factors through its SHI domain.

Bhattacharya Saikat S Levy Michaella J MJ Zhang Ning N Li Hua H Florens Laurence L Washburn Michael P MP Workman Jerry L JL

Nature communications 20210304 1

Heterogeneous ribonucleoproteins (hnRNPs) are RNA binding molecules that are involved in key processes such as RNA splicing and transcription. One such hnRNP protein, hnRNP L, regulates alternative splicing (AS) by binding to pre-mRNA transcripts. However, it is unclear what factors contribute to hnRNP L-regulated AS events. Using proteomic approaches, we identified several key factors that co-purify with hnRNP L. We demonstrate that one such factor, the histone methyltransferase SETD2, specific ...[more]

PMID: 33664260

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