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Integrative structural analysis of NF90-NF45 heterodimers reveals architectural rearrangements and oligomerisation on binding dsRNA

ABSTRACT: EDC Crosslinking Mass Spectrometry with quantitation of NF90-NF45 protein complex and NF45-NF90long-dsRNA complex

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Juan Zou

LAB HEAD: Juri Rappsilber

PROVIDER: PXD053010 | Pride | 2025-05-07

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	NF90_NF45.fasta	Fasta
	Zou_Rappsilber_AC_NF90-NF45-RNA_EDC.xlsx	Xlsx
	Zou_Rappsilber_AC_NF90-NF45-RNA_EDC_S1_R1.mgf	Mgf
	Zou_Rappsilber_AC_NF90-NF45-RNA_EDC_S1_R1.raw	Raw
	Zou_Rappsilber_AC_NF90-NF45-RNA_EDC_S1_R2.mgf	Mgf

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Publications

Integrative structural analysis of NF45-NF90 heterodimers reveals architectural rearrangements and oligomerization on binding dsRNA.

Winterbourne Sophie S Jayachandran Uma U Zou Juan J Rappsilber Juri J Granneman Sander S Cook Atlanta G AG

Nucleic acids research 20250301 6

Complexes of nuclear factors 45 and 90 (NF45-NF90) play a multitude of roles in co- and post-transcriptional RNA processing, including regulating adenosine-to-inosine editing, cassette exon and back splicing, and splicing fidelity. NF45-NF90 complexes recognize double-stranded RNA (dsRNA) and, in human cells, primarily interact with Alu inverted repeats (AluIRs) that are commonly inserted into introns and other non-coding RNA regions. Intronic AluIRs of ∼300 bp can regulate splicing outcomes, su ...[more]

PMID: 40156862

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