4ro1 | pdb_00004ro1
An 3'-5'-exoribonuclease that specifically recognizes RNAs.
Structural highlights
Function[DI3L2_SCHPO] 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'.[HAMAP-Rule:MF_03045][1] Publication Abstract from PubMedAfter deadenylation and decapping, cytoplasmic mRNA can be digested in two opposite directions: in the 5'-3' direction by Xrn1 or in the 3'-5' direction by the exosome complex. Recently, a novel 3'-5' RNA-decay pathway involving Dis3l2 has been described that differs from degradation by Xrn1 and the exosome. The product of the Schizosaccharomyces pombe gene SPAC2C4.07c was identified as a homologue of human Dis3l2. In this work, the 2.8 A resolution X-ray crystal structure of S. pombe Dis3l2 (SpDis3l2) is reported, the conformation of which is obviously different from that in the homologous mouse Dis3l2-RNA complex. Fluorescence polarization assay experiments showed that RNB and S1 are the primary RNA-binding domains and that the CSDs (CSD1 and CSD2) play an indispensable role in the RNA-binding process of SpDis3l2. Taking the structure comparison and mutagenic experiments together, it can be inferred that the RNA-recognition pattern of SpDis3l2 resembles that of its mouse homologue rather than that of the Escherichia coli RNase II-RNA complex. Furthermore, a drastic conformation change could occur following the binding of the RNA substrate to SpDis3l2. Structural analysis of Dis3l2, an exosome-independent exonuclease from Schizosaccharomyces pombe.,Lv H, Zhu Y, Qiu Y, Niu L, Teng M, Li X Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1284-94. doi:, 10.1107/S1399004715005805. Epub 2015 May 14. PMID:26057668[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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