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

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Michaella Levy

LAB HEAD: Laurence Florens

PROVIDER: PXD022946 | Pride | 2021-02-01

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	DTASelect.params	Other
	Hs_Halo_293T-WCE_Halo-AP-1_rKCTi_L1_1.mzid.gz	Mzid
	Hs_Halo_293T-WCE_Halo-AP-1_rKCTi_L1_101.RAW	Raw
	Hs_Halo_293T-WCE_Halo-AP-1_rKCTi_L1_101.mgf	Mgf
	Hs_Halo_293T-WCE_Halo-AP-1_rKCTi_L1_101.ms2	Other

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Publications

Structural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing.

Bhattacharya Saikat S Wang Suman S Reddy Divya D Shen Siyuan S Zhang Ying Y Zhang Ning N Li Hua H Washburn Michael P MP Florens Laurence L Shi Yunyu Y Workman Jerry L JL Li Fudong F

Nature communications 20211108 1

The RNA recognition motif (RRM) binds to nucleic acids as well as proteins. More than one such domain is found in the pre-mRNA processing hnRNP proteins. While the mode of RNA recognition by RRMs is known, the molecular basis of their protein interaction remains obscure. Here we describe the mode of interaction between hnRNP L and LL with the methyltransferase SETD2. We demonstrate that for the interaction to occur, a leucine pair within a highly conserved stretch of SETD2 insert their side chai ...[more]

PMID: 34750379

Publication: 1/2

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