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The carboxy-terminal segment of the human LINE-1 ORF2 protein is involved in RNA binding()

The human LINE-1/L1 ORF2 protein is a multifunctional enzyme which plays a vital role in the life cycle of the human L1 retrotransposon. The protein consists of an endonuclease domain, followed by a central reverse transcriptase domain and a carboxy-terminal C-domain with unknown function. Here, we...

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Detalles Bibliográficos
Autores principales: Piskareva, Olga, Ernst, Christina, Higgins, Niamh, Schmatchenko, Vadim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3821027/
https://www.ncbi.nlm.nih.gov/pubmed/24251107
http://dx.doi.org/10.1016/j.fob.2013.09.005
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author Piskareva, Olga
Ernst, Christina
Higgins, Niamh
Schmatchenko, Vadim
author_facet Piskareva, Olga
Ernst, Christina
Higgins, Niamh
Schmatchenko, Vadim
author_sort Piskareva, Olga
collection PubMed
description The human LINE-1/L1 ORF2 protein is a multifunctional enzyme which plays a vital role in the life cycle of the human L1 retrotransposon. The protein consists of an endonuclease domain, followed by a central reverse transcriptase domain and a carboxy-terminal C-domain with unknown function. Here, we explore the nucleic acid binding properties of the 180-amino acid carboxy-terminal segment (CTS) of the human L1 ORF2p in vitro. In a series of experiments involving gel shift assay, we demonstrate that the CTS of L1 ORF2p binds RNA in non-sequence-specific manner. Finally, we report that mutations destroying the putative Zn-knuckle structure of the protein do not significantly affect the level of RNA binding and discuss the possible functional role of the CTS in L1 retrotransposition.
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spelling pubmed-38210272013-11-18 The carboxy-terminal segment of the human LINE-1 ORF2 protein is involved in RNA binding() Piskareva, Olga Ernst, Christina Higgins, Niamh Schmatchenko, Vadim FEBS Open Bio Article The human LINE-1/L1 ORF2 protein is a multifunctional enzyme which plays a vital role in the life cycle of the human L1 retrotransposon. The protein consists of an endonuclease domain, followed by a central reverse transcriptase domain and a carboxy-terminal C-domain with unknown function. Here, we explore the nucleic acid binding properties of the 180-amino acid carboxy-terminal segment (CTS) of the human L1 ORF2p in vitro. In a series of experiments involving gel shift assay, we demonstrate that the CTS of L1 ORF2p binds RNA in non-sequence-specific manner. Finally, we report that mutations destroying the putative Zn-knuckle structure of the protein do not significantly affect the level of RNA binding and discuss the possible functional role of the CTS in L1 retrotransposition. Elsevier 2013-09-21 /pmc/articles/PMC3821027/ /pubmed/24251107 http://dx.doi.org/10.1016/j.fob.2013.09.005 Text en © 2013 The Authors http://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-No Derivative Works License, which permits non-commercial use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Article
Piskareva, Olga
Ernst, Christina
Higgins, Niamh
Schmatchenko, Vadim
The carboxy-terminal segment of the human LINE-1 ORF2 protein is involved in RNA binding()
title The carboxy-terminal segment of the human LINE-1 ORF2 protein is involved in RNA binding()
title_full The carboxy-terminal segment of the human LINE-1 ORF2 protein is involved in RNA binding()
title_fullStr The carboxy-terminal segment of the human LINE-1 ORF2 protein is involved in RNA binding()
title_full_unstemmed The carboxy-terminal segment of the human LINE-1 ORF2 protein is involved in RNA binding()
title_short The carboxy-terminal segment of the human LINE-1 ORF2 protein is involved in RNA binding()
title_sort carboxy-terminal segment of the human line-1 orf2 protein is involved in rna binding()
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3821027/
https://www.ncbi.nlm.nih.gov/pubmed/24251107
http://dx.doi.org/10.1016/j.fob.2013.09.005
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