ANGEL2 is a member of the CCR4 family of deadenylases with 2′,3′-cyclic phosphatase activity

Author:

Pinto Paola H.1ORCID,Kroupova Alena2ORCID,Schleiffer Alexander3ORCID,Mechtler Karl45ORCID,Jinek Martin2ORCID,Weitzer Stefan1ORCID,Martinez Javier1ORCID

Affiliation:

1. Max Perutz Labs, Medical University of Vienna, Vienna BioCenter, 1030 Vienna, Austria.

2. Department of Biochemistry, University of Zurich, Zurich, Switzerland.

3. IMP/IMBA Bioinformatics Core Facility, Research Institute of Molecular Pathology, Vienna BioCenter, 1030 Vienna, Austria.

4. Research Institute of Molecular Pathology, Vienna BioCenter, 1030 Vienna, Austria.

5. Institute of Molecular Biotechnology (IMBA), Austrian Academy of Sciences, Vienna BioCenter, 1030 Vienna, Austria.

Abstract

Dephosphorylating RNA molecules Transfer RNA (tRNA) and messenger RNA molecules often acquire a terminal 2′,3′-cyclic phosphate group when processed in the cell. These cyclic phosphates provide attachment points for tRNA ligases and must be removed to recycle tRNAs from stalled ribosomes. Pinto et al. identified an enzyme from human tissue culture cells that can do the job. Biochemical characterization and analysis of a crystal structure reveal ANGEL2 as a 2′,3′-cyclic phosphatase with functions for RNA processing and modification. Science , this issue p. 524

Funder

FWF

Fonds zur Forderung der wissenschaftlichen Forschung

Boehringer Ingelheim Fonds PhD Fellowships

National Competence Center for Research (NCCR) RNA and Disease

Horizon 2020 EPIC-XS

Medical University of Vienna

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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