Journal
FEBS OPEN BIO
Volume 12, Issue 5, Pages 1036-1049Publisher
WILEY
DOI: 10.1002/2211-5463.13011
Keywords
AtHESPERIN; circadian rhythms; deadenylation; mRNA decay; poly(A) tail
Categories
Funding
- Operational Programme 'Competitiveness, Entrepreneurship and Innovation' (NSRF) [MIS 5002636]
- European Union (European Regional Development Fund)
- Postgraduate Programs 'Biotechnology - Quality Assessment in Nutrition and the Environment' (University of Thessaly Research Committee, UTH/RC) [3439]
- Department of Biochemistry and Biotechnology, University of Thessaly (DBB/UTH) [UTH/RC 3817]
- DBB/UTH [UTH/RC 5851]
- National Research Foundation
- State Scholarships Foundation (IKY) Fellowship of Excellence for Postgraduate Studies in Greece - Siemens Programme
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This study determined the catalytic site of the circadian deadenylase Hesperin in plants and explored its catalytic mechanism and efficiency. The findings contribute to the understanding of the intricate mechanisms of circadian mRNA turnover.
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.
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