title: Non-coding Y RNAs as tethers and gates: Insights from bacteria.
abstract: Non-coding RNAs (ncRNAs) called Y RNAs are abundant components of both animal cells and a variety of bacteria. In all species examined, these ~100 nt RNAs are bound to the Ro 60 kDa (Ro60) autoantigen, a ring-shaped protein that also binds misfolded ncRNAs in some vertebrate nuclei. Although the function of Ro60 RNPs has been mysterious, we recently reported that a bacterial Y RNA tethers Ro60 to the 3' to 5' exoribonuclease polynucleotide phosphorylase (PNPase) to form RYPER (Ro60/Y RNA/PNPase Exoribonuclease RNP), a new RNA degradation machine. PNPase is a homotrimeric ring that degrades single-stranded RNA, and Y RNA-mediated tethering of Ro60 increases the effectiveness of PNPase in degrading structured RNAs. Single particle electron microscopy of RYPER suggests that RNA threads through the Ro60 ring into the PNPase cavity. Further studies indicate that Y RNAs may also act as gates to regulate entry of RNA substrates into the Ro60 channel. These findings reveal novel functions for Y RNAs and raise questions about how the bacterial findings relate to the roles of these ncRNAs in animal cells. Here we review the literature on Y RNAs, highlighting their close relationship with Ro60 proteins and the hypothesis that these ncRNAs function generally to tether Ro60 rings to diverse RNA-binding proteins.
authors.affiliation: Department of Cell Biology; Yale School of Medicine; New Haven, CT USA; Department of Molecular Biophysics and Biochemistry; Yale School of Medicine; New Haven, CT USA.
authors.forename: Sandra L
authors.initials: SL
authors.lastname: Wolin
authors.affiliation: Department of Cell Biology; Yale School of Medicine; New Haven, CT USA.
authors.forename: Cedric
authors.initials: C
authors.lastname: Belair
authors.affiliation: Department of Cell Biology; Yale School of Medicine; New Haven, CT USA.
authors.forename: Marco
authors.initials: M
authors.lastname: Boccitto
authors.affiliation: Department of Cell Biology; Yale School of Medicine; New Haven, CT USA.
authors.forename: Xinguo
authors.initials: X
authors.lastname: Chen
authors.affiliation: Department of Cell Biology; Yale School of Medicine; New Haven, CT USA.
authors.forename: Soyeong
authors.initials: S
authors.lastname: Sim
authors.affiliation: Department of Molecular Biophysics and Biochemistry; Yale School of Medicine; New Haven, CT USA.
authors.forename: David W
authors.initials: DW
authors.lastname: Taylor
authors.affiliation: Department of Molecular Biophysics and Biochemistry; Yale School of Medicine; New Haven, CT USA; Tsinghua-Peking Center for Life Sciences; School of Life Sciences; Tsinghua University; Beijing, P.R. China.
authors.forename: Hong-Wei
authors.initials: HW
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D022661:RNA, Untranslated / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism
chemical_list: D022661:RNA, Untranslated; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins
keywords: RNA degradation; RYPER; Y RNAs; exoribonucleases; non-coding RNAs
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