首页    期刊浏览 2024年11月29日 星期五
登录注册

文章基本信息

  • 标题:In vivo 3′-to-5′ exoribonuclease targetomes of Streptococcus pyogenes
  • 作者:Anne-Laure Lécrivain ; Anaïs Le Rhun ; Thibaud T. Renault
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2018
  • 卷号:115
  • 期号:46
  • 页码:11814-11819
  • DOI:10.1073/pnas.1809663115
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要: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 Streptococcus pyogenes . We determined that YhaM is an unspecific enzyme that trims a few nucleotides and targets the majority of transcript ends, generated either by transcription termination or by endonucleolytic activity. The molecular determinants for YhaM-limited processivity are yet to be deciphered. We showed that PNPase clears the cell from mRNA decay fragments produced by endoribonucleases (endoRNases) and is the major 3′-to-5′ exoRNase for RNA turnover in S. pyogenes . In particular, PNPase is responsible for the degradation of regulatory elements from 5′ untranslated regions. However, we observed little RNase R activity in standard culture conditions. Overall, our study sheds light on the very distinct features of S. pyogenes 3′-to-5′ exoRNases.
  • 关键词:3′-to-5′ exoRNase ; 5′-end sequencing ; 3′-end sequencing ; Streptococcus pyogenes ; RNA degradation
Loading...
联系我们|关于我们|网站声明
国家哲学社会科学文献中心版权所有