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RBM7 subunit of the NEXT complex binds U-rich sequences and targets 3 '-end extended forms of snRNAs

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HROŠŠOVÁ Dominika ŠIKORSKÝ Tomáš POTĚŠIL David BARTOŠOVIČ Marek PASULKA Josef ZDRÁHAL Zbyněk ŠTEFL Richard VAŇÁČOVÁ Štěpánka

Druh Článek v odborném periodiku
Časopis / Zdroj Nucleic Acids Research
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www http://nar.oxfordjournals.org/content/43/8/4236.full.pdf+html
Doi http://dx.doi.org/10.1093/nar/gkv240
Obor Biochemie
Klíčová slova RNA-POLYMERASE-II; CRYPTIC UNSTABLE TRANSCRIPTS; STRUCTURAL BASIS; SPLICING REGULATION; POLY(A) POLYMERASE; PROTEOMIC ANALYSIS; PROTEIN-STRUCTURE; QUALITY-CONTROL; EXOSOME; RECOGNITION
Popis The Nuclear Exosome Targeting (NEXT) complex is a key cofactor of the mammalian nuclear exosome in the removal of Promoter Upstream Transcripts (PROMPTs) and potentially aberrant forms of other noncoding RNAs, such as snRNAs. NEXT is composed of three subunits SKIV2L2, ZCCHC8 and RBM7. We have recently identified the NEXT complex in our screen for oligo(U) RNA-binding factors. Here, we demonstrate that NEXT displays preference for U-rich pyrimidine sequences and this RNA binding is mediated by the RNA recognition motif (RRM) of the RBM7 subunit. We solved the structure of RBM7 RRM and identified two phenylalanine residues that are critical for interaction with RNA. Furthermore, we showed that these residues are required for the NEXT interaction with snRNAs in vivo. Finally, we show that depletion of components of the NEXT complex alone or together with exosome nucleases resulted in the accumulation of mature as well as extended forms of snRNAs. Thus, our data suggest a new scenario in which the NEXT complex is involved in the surveillance of snRNAs and/or biogenesis of snRNPs.
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