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The role of 3'-5' exoribonucleases in RNA degradation.
Andrade, José M; Pobre, Vânia; Silva, Inês J; Domingues, Susana; Arraiano, Cecília M.
Afiliación
  • Andrade JM; Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Qeiras, Portugal.
Prog Mol Biol Transl Sci ; 85: 187-229, 2009.
Article en En | MEDLINE | ID: mdl-19215773
RNA degradation is a major process controlling RNA levels and plays a central role in cell metabolism. From the labile messenger RNA to the more stable noncoding RNAs (mostly rRNA and tRNA, but also the expanding class of small regulatory RNAs) all molecules are eventually degraded. Elimination of superfluous transcripts includes RNAs whose expression is no longer required, but also the removal of defective RNAs. Consequently, RNA degradation is an inherent step in RNA quality control mechanisms. Furthermore, it contributes to the recycling of the nucleotide pool in the cell. Escherichia coli has eight 3'-5' exoribonucleases, which are involved in multiple RNA metabolic pathways. However, only four exoribonucleases appear to accomplish all RNA degradative activities: polynucleotide phosphorylase (PNPase), ribonuclease II (RNase II), RNase R, and oligoribonuclease. Here, we summarize the available information on the role of bacterial 3'-5' exoribonucleases in the degradation of different substrates, highlighting the most recent data that have contributed to the understanding of the diverse modes of operation of these degradative enzymes.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Estabilidad del ARN / Escherichia coli / Exorribonucleasas Idioma: En Revista: Prog Mol Biol Transl Sci Asunto de la revista: BIOLOGIA MOLECULAR Año: 2009 Tipo del documento: Article País de afiliación: Portugal Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Estabilidad del ARN / Escherichia coli / Exorribonucleasas Idioma: En Revista: Prog Mol Biol Transl Sci Asunto de la revista: BIOLOGIA MOLECULAR Año: 2009 Tipo del documento: Article País de afiliación: Portugal Pais de publicación: Países Bajos