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The RNase II/RNB family of exoribonucleases: putting the ‘Dis’ in disease

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Important findings over the last years have shed new light onto the mechanistic details of RNA degradation by members of the RNase II/RNB family of exoribonucleases. Members of this family have been shown to be involved in growth, normal chloroplast biogenesis, mitotic control and cancer. Recently, different publications have linked human orthologs (Dis3 and Dis3L2) to important human diseases. This article describes the structural and biochemical characteristics of members of this family of enzymes, and the physiological implications that relate them with disease. WIREs RNA 2013, 4:607–615. doi: 10.1002/wrna.1180 This article is categorized under: RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms RNA Turnover and Surveillance > Regulation of RNA Stability RNA in Disease and Development > RNA in Disease

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Domain organization of members of the RNase II family of enzymes. Members of this family have a similar modular domain organization. The N‐terminal region is variable but shares CSD1 and CSD2, followed by a RNB domain and an S1 domain. At the N‐terminus, S. cerevisiae Dis3/Rrp44 and some other members also contain a conserved CR3 motif and a catalytic PIN domain.
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RNase II family proteins and their role in disease. In the left, the circle indicates human diseases that have been related with mutations in the Dis3 or Dis3L2 proteins. In the right, the circle indicates human pathogens whose physiology has been shown to be affected by mutations in RNase II and/or RNase R. The sections in the outer circle do not correlate with those of the inner circles.
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RNA in Disease and Development > RNA in Disease
RNA Turnover and Surveillance > Regulation of RNA Stability
RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms
RNA Turnover and Surveillance

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