<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>115(46)</volume><submitter>Lecrivain AL</submitter><pubmed_abstract>mRNA decay plays an essential role in the control of gene expression in bacteria. Exoribonucleases (exoRNases), which trim transcripts starting from the 5' or 3' end, are particularly important to fully degrade unwanted transcripts and renew the pool of nucleotides available in the cell. While recent techniques have allowed genome-wide identification of ribonuclease (RNase) targets in bacteria in vivo, none of the 3'-to-5' exoRNase targetomes (i.e., global processing sites) have been studied so far. Here, we report the targetomes of YhaM, polynucleotide phosphorylase (PNPase), and RNase R of the human pathogen &lt;i>Streptococcus pyogenes&lt;/i> We determined that YhaM is an unspecific enzyme that trims a few nucleotides and targets the majority of transcript ends, generated either by transcript</pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pagination>11814-11819</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6243249</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>In vivo 3'-to-5' exoribonuclease targetomes of &lt;i>Streptococcus pyogenes&lt;/i>.</pubmed_title><pmcid>PMC6243249</pmcid><pubmed_authors>Ahmed-Begrich R</pubmed_authors><pubmed_authors>Lecrivain AL</pubmed_authors><pubmed_authors>Renault TT</pubmed_authors><pubmed_authors>Charpentier E</pubmed_authors><pubmed_authors>Le Rhun A</pubmed_authors><pubmed_authors>Hahnke K</pubmed_authors></additional><is_claimable>false</is_claimable><name>In vivo 3'-to-5' exoribonuclease targetomes of &lt;i>Streptococcus pyogenes&lt;/i>.</name><description>mRNA decay plays an essential role in the control of gene expression in bacteria. Exoribonucleases (exoRNases), which trim transcripts starting from the 5' or 3' end, are particularly important to fully degrade unwanted transcripts and renew the pool of nucleotides available in the cell. While recent techniques have allowed genome-wide identification of ribonuclease (RNase) targets in bacteria in vivo, none of the 3'-to-5' exoRNase targetomes (i.e., global processing sites) have been studied so far. Here, we report the targetomes of YhaM, polynucleotide phosphorylase (PNPase), and RNase R of the human pathogen &lt;i>Streptococcus pyogenes&lt;/i> We determined that YhaM is an unspecific enzyme that trims a few nucleotides and targets the majority of transcript ends, generated either by transcript</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Nov</publication><modification>2026-05-06T05:58:36.035Z</modification><creation>2025-05-18T13:32:58.962Z</creation></dates><accession>S-EPMC6243249</accession><cross_references><pubmed>30381461</pubmed><doi>10.1073/pnas.1809663115</doi></cross_references></HashMap>