Research Papers:
Beyond the 3′UTR binding–microRNA-induced protein truncation via DNA binding
PDF | HTML | Supplementary Files | How to cite
Metrics: PDF 1381 views | HTML 2490 views | ?
Abstract
Melanie von Brandenstein1, Stephan H. Bernhart5, Andreas Pansky3, Claudia Richter2, Tobias Kohl1, Martina Deckert4, Axel Heidenreich1, Peter F. Stadler5, Manuel Montesinos-Rongen4,* and Jochen W.U. Fries2,*
1Department of Urology, University Hospital of Cologne, Cologne, Germany
2Institute of Pathology, University Hospital of Cologne, Cologne, Germany
3Department of Natural Sciences, University of Applied Sciences Bonn-Rhein-Sieg, Rheinbach, Germany
4Institute of Neuropathology, University Hospital of Cologne, Cologne, Germany
5Bioinformatics Group, Department of Computer Science and Interdisciplinary Center of Bioinformatics, Leipzig University, Leipzig, Germany
*Co-senior authors
Correspondence to:
Manuel Montesinos-Rongen, email: [email protected]
Melanie von Brandenstein, email: [email protected]
Keywords: Vim3; Mxi-2; miR-498; miR-15; DNA interaction
Received: May 23, 2018 Accepted: August 04, 2018 Published: August 28, 2018
ABSTRACT
Here, we present a miR mechanism which is active in the nucleus and is essential for the production of intron included, C-terminal truncated and biologically active proteins, like e.g. Vim3. We exemplified this mechanism by miRs, miR-15a and miR-498, which are overexpressed in clear cell renal carcinoma or oncocytoma.
Both miRs directly interact with DNA in an intronic region, leading to transcriptional stop, and therefore repress the full length version of the pre-mRNA, resulting in intron included truncated proteins (Mxi-2 and Vim3). A computational survey shows that this miR:DNA interactions mechanism may be generally involved in regulating the human transcriptome, with putative interaction sites in intronic regions for over 1000 genes.
In this work, an entirely new mechanism is revealed how miRs can repress full length protein translation, resulting in C-terminal truncated proteins.
All site content, except where otherwise noted, is licensed under a Creative Commons Attribution 4.0 License.
PII: 26023