{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Singh J"],"funding":["Science and Engineering Research Board","Jamsetji Tata Trust","Department of Biotechnology","DBT/Wellcome Trust India Alliance","Wellcome Trust/DBT India Alliance Fellowship","Wellcome Trust","DBT-IISc Partnership Program Phase-II"],"pagination":["11712-11726"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9723500"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["50(20)"],"pubmed_abstract":["Initiation factor 3 (IF3) regulates the fidelity of bacterial translation initiation by debarring the use of non-canonical start codons or non-initiator tRNAs and prevents premature docking of the 50S ribosomal subunit to the 30S pre-initiation complex (PIC). The C-terminal domain (CTD) of IF3 can carry out most of the known functions of IF3 and sustain Escherichia coli growth. However, the roles of the N-terminal domain (NTD) have remained unclear. We hypothesized that the interaction between NTD and initiator tRNAfMet (i-tRNA) is essential to coordinate the movement of the two domains during the initiation pathway to ensure fidelity of the process. Here, using atomistic molecular dynamics (MD) simulation, we show that R25A/Q33A/R66A mutations do not impact NTD structure but disrupt its i"],"journal":["Nucleic acids research"],"pubmed_title":["The initiation factor 3 (IF3) residues interacting with initiator tRNA elbow modulate the fidelity of translation initiation and growth fitness in Escherichia coli."],"pmcid":["PMC9723500"],"funding_grant_id":["BT/PR13522","R(HR)Tata Chairs/2020–854/78","BT/PR27952-INF/22/212/2018","BT/PR28058","EMR/2016/005617","IA/I/17/2/503313"],"pubmed_authors":["Mishra RK","Singh J","Ayyub SA","Hussain T","Varshney U"],"additional_accession":[]},"is_claimable":false,"name":"The initiation factor 3 (IF3) residues interacting with initiator tRNA elbow modulate the fidelity of translation initiation and growth fitness in Escherichia coli.","description":"Initiation factor 3 (IF3) regulates the fidelity of bacterial translation initiation by debarring the use of non-canonical start codons or non-initiator tRNAs and prevents premature docking of the 50S ribosomal subunit to the 30S pre-initiation complex (PIC). The C-terminal domain (CTD) of IF3 can carry out most of the known functions of IF3 and sustain Escherichia coli growth. However, the roles of the N-terminal domain (NTD) have remained unclear. We hypothesized that the interaction between NTD and initiator tRNAfMet (i-tRNA) is essential to coordinate the movement of the two domains during the initiation pathway to ensure fidelity of the process. Here, using atomistic molecular dynamics (MD) simulation, we show that R25A/Q33A/R66A mutations do not impact NTD structure but disrupt its i","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-28T00:40:19.659Z","creation":"2025-04-04T23:36:55.546Z"},"accession":"S-EPMC9723500","cross_references":{"pubmed":["36399509"],"doi":["10.1093/nar/gkac1053"]}}