Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex

Carlos Frazão, Colin E. McVey, Mónica Amblar, Ana Barbas, Clemens Vonrhein, Cecília M. Arraiano and Maria A. Carrondo ()
Additional contact information
Carlos Frazão: Division of Biological Chemistry
Colin E. McVey: Division of Biological Chemistry
Mónica Amblar: ITQB–Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apt. 127
Ana Barbas: ITQB–Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apt. 127
Clemens Vonrhein: Global Phasing Limited, Sheraton House, Castle Park
Cecília M. Arraiano: ITQB–Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apt. 127
Maria A. Carrondo: Division of Biological Chemistry

Nature, 2006, vol. 443, issue 7107, 110-114

Abstract: Keeping RNA up to scratch RNA degradation by class II RNase family members plays a fundamental role in the maturation, turnover and quality control of RNA. The crystal structure of an RNase II has now been determined for the first time, in both RNA bound and ligand free forms. Surprisingly, the domain structure does not correspond to that predicted by sequence analysis. The molecule has two points of contact with the RNA: one site anchors the RNA, and the other catalyses cleavage. The structural details explain why RNase II acts only on single-stranded RNA, and how it moves along the RNA to processively degrade it.

Date: 2006
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DOI: 10.1038/nature05080

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