AI Article Synopsis
- Scavenger decapping enzymes (DcpS) play a crucial role in breaking down mRNA by targeting the cap structure m(7)GpppN, which is a common feature in eukaryotic mRNA.
- The study explores how different substitutions at the N7 position of the guanine in the cap structure affect DcpS from various organisms, including humans and some nematodes, focusing on their rate of hydrolysis and binding affinities.
- Findings indicate that the DcpS enzyme has a flexible cap-binding pocket, allowing it to accommodate various substrates with different N7 structural modifications for effective hydrolysis.
Article Abstract
Scavenger decapping enzymes (DcpS) are involved in eukaryotic mRNA degradation process. They catalyze the cleavage of residual cap structure m(7)GpppN and/or short capped oligonucleotides resulting from exosom-mediated the 3' to 5' digestion. For the specific cap recognition and efficient degradation by DcpS, the positive charge at N7 position of guanine moiety is required. Here we examine the role the N7 substitution within the cap structure on the interactions with DcpS (human, Caenorhabditis elegans and Ascaris suum) comparing the hydrolysis rates of dinucleotide cap analogs (m(7)GpppG, et(7)GpppG, but(7)GpppG, bn(7)GpppG) and the binding affinities of hydrolysis products (m(7)GMP, et(7)GMP, but(7)GMP, bn(7)GMP). Our results show the conformational flexibility of the region within DcpS cap-binding pocket involved in the interaction with N7 substituted guanine, which enables accommodation of substrates with differently sized N7 substituents.
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| http://dx.doi.org/10.1016/j.bbrc.2015.06.001 | DOI Listing |
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