PXD049390-1

PXD049390 is an original dataset announced via ProteomeXchange.

Title	Identification of potential readers for eukaryotic internal mRNA N7-methylguanosine (m7G) modification
Description	The project aims to identify the RNA binding proteins that can specifically bind to mRNA internal modification N7-methylguanosine (m7G). N7-methylguanosine (m7G) methylation has been long identified as the essential cap modification for eukaryotic mRNA, but later has been identified internally in various types of RNAs, including tRNA, rRNA, miRNA, and mRNA. While the METTL1/WDR4 complex, responsible for tRNA m7G installation, has been suggested to be responsible for internal mRNA modification as well, little is known about the proteins that can identify and interact with m7G. To better understand its interaction with RNA binding proteins and further define its regulatory function in mRNA metabolism, we performed the experiment to pulldown proteins with different binding affinity on unmodified G and m7G and subject the enriched fractions to mass spectrometry.
HostingRepository	PRIDE
AnnounceDate	2024-09-03
AnnouncementXML	Submission_2024-09-02_23:49:55.961.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD049390
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Chang Liu
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2024-02-14 13:09:30	ID requested
⏵ 1	2024-09-02 23:49:56	announced

10.1038/S41467-024-51634-W;

10.6019/PXD049390;

submitter keyword: mRNA modification,N7-methylguanosine

Chuan He
contact affiliation	The University of Chicago
contact email	chuanhe@uchicago.edu
lab head
Chang Liu
contact affiliation	The University of Chicago
contact email	changliu0024@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD049390
     1. Label: PRIDE project
     2. Name: Identification of potential readers for eukaryotic internal mRNA N7-methylguanosine (m7G) modification