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10.1038/s41467-020-19326-3

http://scihub22266oqcxt.onion/10.1038/s41467-020-19326-3
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suck abstract from ncbi


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pmid33139726      Nat+Commun 2020 ; 11 (1): 5508
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  • Extensive 5 -surveillance guards against non-canonical NAD-caps of nuclear mRNAs in yeast #MMPMID33139726
  • Zhang Y; Kuster D; Schmidt T; Kirrmaier D; Nubel G; Ibberson D; Benes V; Hombauer H; Knop M; Jaschke A
  • Nat Commun 2020[Nov]; 11 (1): 5508 PMID33139726show ga
  • The ubiquitous redox coenzyme nicotinamide adenine dinucleotide (NAD) acts as a non-canonical cap structure on prokaryotic and eukaryotic ribonucleic acids. Here we find that in budding yeast, NAD-RNAs are abundant (>1400 species), short (<170 nt), and mostly correspond to mRNA 5'-ends. The modification percentage of transcripts is low (<5%). NAD incorporation occurs mainly during transcription initiation by RNA polymerase II, which uses distinct promoters with a YAAG core motif for this purpose. Most NAD-RNAs are 3'-truncated. At least three decapping enzymes, Rai1, Dxo1, and Npy1, guard against NAD-RNA at different cellular locations, targeting overlapping transcript populations. NAD-mRNAs are not translatable in vitro. Our work indicates that in budding yeast, most of the NAD incorporation into RNA seems to be disadvantageous to the cell, which has evolved a diverse surveillance machinery to prematurely terminate, decap and reject NAD-RNAs.
  • |5' Untranslated Regions[MESH]
  • |Cell Nucleus/genetics[MESH]
  • |Endoribonucleases/*metabolism[MESH]
  • |NAD/*metabolism[MESH]
  • |Pyrophosphatases/metabolism[MESH]
  • |RNA Caps/*metabolism[MESH]
  • |RNA Stability[MESH]
  • |RNA, Messenger/*metabolism[MESH]
  • |RNA-Binding Proteins/metabolism[MESH]
  • |Ribosomes/metabolism[MESH]
  • |Saccharomyces cerevisiae Proteins/metabolism[MESH]
  • |Saccharomyces cerevisiae/*genetics/metabolism[MESH]


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