title: Endoribonucleases--enzymes gaining spotlight in mRNA metabolism.
abstract: The efficient turnover of messenger RNA represents an important mechanism that allows the cell to control gene expression. Until recently, the mechanism of mRNA decay was mainly attributed to exonucleases, comprising enzymes that degrade RNAs from the ends of the molecules. This article summarizes the endoribonucleases, comprising enzymes that cleave RNA molecules internally, which were identified in more recent years in eukaryotic mRNA metabolism. Endoribonucleases have received little attention in the past, based on the difficulty in their identification and a lack of understanding of their physiological significance. This review aims to compare the similarities and differences among this group of enzymes, as well as their known cellular functions. Despite the many differences in protein structure, and thus difficulties in identifying them based on amino acid sequence, most endoribonucleases possess essential cellular functions and have been shown to play an important role in mRNA turnover.
authors.affiliation: Chemistry Program, University of Northern British Columbia, Prince George, BC, Canada.
authors.forename: Wai Ming
authors.initials: WM
authors.lastname: Li
authors.forename: Tavish
authors.initials: T
authors.lastname: Barnes
authors.forename: Chow H
authors.initials: CH
authors.lastname: Lee
mesh_terms: D000818:Animals; D060565:Argonaute Proteins; D002352:Carrier Proteins / Q000378:metabolism; D004265:DNA Helicases; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase / Q000378:metabolism; D004722:Endoribonucleases / Q000378:metabolism*; D015852:Eukaryotic Initiation Factor-2 / Q000378:metabolism; D063326:Exosome Multienzyme Ribonuclease Complex; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D000075223:Poly-ADP-Ribose Binding Proteins; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D020365:RNA Helicases; D000067776:RNA Recognition Motif Proteins; D020871:RNA Stability; D012333:RNA, Messenger / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism; D043244:Ribonuclease III / Q000378:metabolism; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D019098:Telomerase / Q000378:metabolism
chemical_list: C466422:AGO2 protein, human; D060565:Argonaute Proteins; D002352:Carrier Proteins; D015852:Eukaryotic Initiation Factor-2; D008565:Membrane Proteins; D000075223:Poly-ADP-Ribose Binding Proteins; D000067776:RNA Recognition Motif Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D029701:Saccharomyces cerevisiae Proteins; C403982:ERN2 protein, human; D017346:Protein Serine-Threonine Kinases; D019098:Telomerase; D004722:Endoribonucleases; D063326:Exosome Multienzyme Ribonuclease Complex; C512261:SMG6 protein, human; C116181:polysomal RNase 1; C542283:DIS3 protein, S cerevisiae; C031956:2-5A-dependent ribonuclease; D043244:Ribonuclease III; C046366:angiogenin; D012259:Ribonuclease, Pancreatic; D010749:Phosphoprotein Phosphatases; C097081:PPP1R8 protein, human; D004265:DNA Helicases; C116070:G3BP1 protein, human; D020365:RNA Helicases; D005634:Fructose-Bisphosphate Aldolase; C085108:APEX1 protein, human; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase