{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Beta RAA"],"funding":["University of Thessaly Research Committee","National Research Foundation","State Scholarships Foundation (IKY) Fellowship of Excellence for Postgraduate Studies in Greece - Siemens Programme (to AK)","OMIC-ENGINE (MIS 5002636) implemented under \"Reinforcement of the Research and Innovation Infrastructure\", Operational Programme \"Competitiveness, Entrepreneurship and Innovation\" (NSRF 2014-2020)","European Regional Development Fund"],"pagination":["1036-1049"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9063446"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(5)"],"pubmed_abstract":["The 24-h molecular clock is based on the stability of rhythmically expressed transcripts. The shortening of the poly(A) tail of mRNAs is often the first and rate-limiting step that determines the lifespan of a mRNA and is catalyzed by deadenylases. Herein, we determine the catalytic site of Hesperin, a recently described circadian deadenylase in plants, using a modified site-directed mutagenesis protocol and a custom vector, pATHRA. To explore the catalytic efficiency of AtHESPERIN, we investigated the effect of AMP and neomycin, and used molecular modeling simulations to propose a catalytic mechanism. Collectively, the biochemical and in silico results classify AtHESPERIN in the exonuclease-endonuclease-phosphatase deadenylase superfamily and contribute to the understanding of the intricate mechanisms of circadian mRNA turnover."],"journal":["FEBS open bio"],"pubmed_title":["Biochemical and in silico identification of the active site and the catalytic mechanism of the circadian deadenylase HESPERIN."],"pmcid":["PMC9063446"],"funding_grant_id":["3439","3817","5851","MIS 5002636"],"pubmed_authors":["Leonidas DD","Douka V","Balatsos NAA","Kyritsis A","Beta RAA","Vlachakis D","Papanastasi E","Rizouli M"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical and in silico identification of the active site and the catalytic mechanism of the circadian deadenylase HESPERIN.","description":"The 24-h molecular clock is based on the stability of rhythmically expressed transcripts. The shortening of the poly(A) tail of mRNAs is often the first and rate-limiting step that determines the lifespan of a mRNA and is catalyzed by deadenylases. Herein, we determine the catalytic site of Hesperin, a recently described circadian deadenylase in plants, using a modified site-directed mutagenesis protocol and a custom vector, pATHRA. To explore the catalytic efficiency of AtHESPERIN, we investigated the effect of AMP and neomycin, and used molecular modeling simulations to propose a catalytic mechanism. Collectively, the biochemical and in silico results classify AtHESPERIN in the exonuclease-endonuclease-phosphatase deadenylase superfamily and contribute to the understanding of the intricate mechanisms of circadian mRNA turnover.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2026-05-31T06:00:41.759Z","creation":"2025-02-19T01:55:00.471Z"},"accession":"S-EPMC9063446","cross_references":{"pubmed":["33095977"],"doi":["10.1002/2211-5463.13011"]}}