In Vivo and In Vitro Characterization of the RNA Binding Capacity of SETD1A (KMT2F)

For several histone lysine methyltransferases (HKMTs), RNA binding has been already shown to be a functionally relevant feature, but detailed information on the RNA interactome of these proteins is not always known. Of the six human KMT2 proteins responsible for the methylation of the H3K4 residue,...

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Bibliographic Details
Published in:International journal of molecular sciences 2023-11, Vol.24 (22), p.16032
Main Authors: Amin, Harem Muhamad, Szabo, Beata, Abukhairan, Rawan, Zeke, Andras, Kardos, József, Schad, Eva, Tantos, Agnes
Format: Article
Language:English
Subjects:
Analysis
Datasets
DNA damage
DNA methylation
Enzymes
Experiments
Genes
histone lysine methyltransferase
Insects
KMT2F
Lysine
Methylation
Methyltransferases
Mutation
non-coding RNA
Pharmaceutical industry
Proteins
RNA
RNA binding
RRM domain
Schizophrenia
Scientific equipment and supplies industry
SETD1A
Stem cells
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Summary:For several histone lysine methyltransferases (HKMTs), RNA binding has been already shown to be a functionally relevant feature, but detailed information on the RNA interactome of these proteins is not always known. Of the six human KMT2 proteins responsible for the methylation of the H3K4 residue, two—SETD1A and SETD1B—contain RNA recognition domains (RRMs). Here we investigated the RNA binding capacity of SETD1A and identified a broad range of interacting RNAs within HEK293T cells. Our analysis revealed that similar to yeast Set1, SETD1A is also capable of binding several coding and non-coding RNAs, including RNA species related to RNA processing. We also show direct RNA binding activity of the individual RRM domain in vitro, which is in contrast with the RRM domain found in yeast Set1. Structural modeling revealed important details on the possible RNA recognition mode of SETD1A and highlighted some fundamental differences between SETD1A and Set1, explaining the differences in the RNA binding capacity of their respective RRMs.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms242216032