The extended AT-hook is a novel RNA binding motif

Filarsky, Michael and Zillner, Karina and Araya, Ingrid and Villar-Garea, Ana and Merkl, Rainer and Laengst, Gernot and Nemeth, Attila (2015) The extended AT-hook is a novel RNA binding motif. RNA BIOLOGY, 12 (8). pp. 864-876. ISSN 1547-6286, 1555-8584

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Abstract

The AT-hook has been defined as a DNA binding peptide motif that contains a glycine-arginine-proline (G-R-P) tripeptide core flanked by basic amino acids. Recent reports documented variations in the sequence of AT-hooks and revealed RNA binding activity of some canonical AT-hooks, suggesting a higher structural and functional variability of this protein domain than previously anticipated. Here we describe the discovery and characterization of the extended AT-hook peptide motif (eAT-hook), in which basic amino acids appear symmetrical mainly at a distance of 12-15 amino acids from the G-R-P core. We identified 80 human and 60 mouse eAT-hook proteins and biochemically characterized the eAT-hooks of Tip5/BAZ2A, PTOV1 and GPBP1. Microscale thermophoresis and electrophoretic mobility shift assays reveal the nucleic acid binding features of this peptide motif, and show that eAT-hooks bind RNA with one order of magnitude higher affinity than DNA. In addition, cellular localization studies suggest a role for the N-terminal eAT-hook of PTOV1 in nucleocytoplasmic shuttling. In summary, our findings classify the eAT-hook as a novel nucleic acid binding motif, which potentially mediates various RNA-dependent cellular processes.

Item Type: Article
Uncontrolled Keywords: DNA-BINDING; PROSTATE-CANCER; GENOMIC DATA; PROTEIN; TRANSCRIPTION; CHROMATIN; DOMAIN; SIGNALS; PTOV1; HMGA1; AT-hook; GPBP1; microscale thermophoresis; protein-RNA interaction; PTOV1; RNA-binding domain; Tip5
Subjects: 500 Science > 570 Life sciences
Divisions: Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie
Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie
Depositing User: Dr. Gernot Deinzer
Date Deposited: 14 Jun 2019 12:34
Last Modified: 14 Jun 2019 12:34
URI: https://pred.uni-regensburg.de/id/eprint/5041

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