In Vivo and In Vitro Characterization of the RNA Binding Capacity of SETD1A (KMT2F).
KMT2F
RNA binding
RNA immunoprecipitation
RRM domain
SETD1A
histone lysine methyltransferase
microscale thermophoresis
non-coding RNA
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
07 Nov 2023
07 Nov 2023
Historique:
received:
25
09
2023
revised:
03
11
2023
accepted:
05
11
2023
medline:
27
11
2023
pubmed:
25
11
2023
entrez:
25
11
2023
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 38003223
pii: ijms242216032
doi: 10.3390/ijms242216032
pmc: PMC10671326
pii:
doi:
Substances chimiques
RNA
63231-63-0
Saccharomyces cerevisiae Proteins
0
Setd1A protein, human
EC 2.1.1.43
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : National Research, Development and Innovation Office, Hungary
ID : K142851
Organisme : National Research, Development and Innovation Office, Hungary
ID : K138937
Organisme : Hungarian Academy of Sciences
ID : NAP2022-I-3/2022
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