title: Intracellular ribonucleases involved in transcript processing and decay: precision tools for RNA.
abstract: In order to adapt to changing environmental conditions and regulate intracellular events such as division, cells are constantly producing new RNAs while discarding old or defective transcripts. These functions require the coordination of numerous ribonucleases that precisely cleave and trim newly made transcripts to produce functional molecules, and rapidly destroy unnecessary cellular RNAs. In recent years our knowledge of the nature, functions and structures of these enzymes in bacteria, archaea and eukaryotes has dramatically expanded. We present here a synthetic overview of the recent development in this dynamic area which has seen the identification of many new endoribonucleases and exoribonucleases. Moreover, the increasing pace at which the structures of these enzymes, or of their catalytic domains, have been solved has provided atomic level detail into their mechanisms of action. Based on sequence conservation and structural data, these proteins have been grouped into families, some of which contain only ribonuclease members, others including a variety of nucleolytic enzymes that act upon DNA and/or RNA. At the other extreme some ribonucleases belong to families of proteins involved in a wide variety of enzymatic reactions. Functional characterization of these fascinating enzymes has provided evidence for the extreme diversity of their biological functions that include, for example, removal of poly(A) tails (deadenylation) or poly(U) tails from eukaryotic RNAs, processing of tRNA and mRNA 3' ends, maturation of rRNAs and destruction of unnecessary mRNAs. This article is part of a Special Issue entitled: RNA Decay mechanisms.
authors.affiliation: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
authors.forename: Cecília Maria
authors.initials: CM
authors.lastname: Arraiano
authors.forename: Fabienne
authors.initials: F
authors.lastname: Mauxion
authors.forename: Sandra Cristina
authors.initials: SC
authors.lastname: Viegas
authors.forename: Rute Gonçalves
authors.initials: RG
authors.lastname: Matos
authors.forename: Bertrand
authors.initials: B
authors.lastname: Séraphin
mesh_terms: D001105:Archaea / Q000201:enzymology; D004247:DNA / Q000235:genetics; D004722:Endoribonucleases / Q000737:chemistry / Q000145:classification / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology; D005095:Exoribonucleases / Q000737:chemistry / Q000145:classification / Q000235:genetics*; D006801:Humans; D011487:Protein Conformation; D017434:Protein Structure, Tertiary / Q000235:genetics; D020871:RNA Stability / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics*
chemical_list: D012333:RNA, Messenger; D004247:DNA; D004722:Endoribonucleases; D005095:Exoribonucleases