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Solution Structure of an Archaeal DNA Binding Protein with an Eukaryotic Zinc Finger Fold

While the basal transcription machinery in archaea is eukaryal-like, transcription factors in archaea and their viruses are usually related to bacterial transcription factors. Nevertheless, some of these organisms show predicted classical zinc fingers motifs of the C2H2 type, which are almost exclus...

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Autores principales: Guillière, Florence, Danioux, Chloé, Jaubert, Carole, Desnoues, Nicole, Delepierre, Muriel, Prangishvili, David, Sezonov, Guennadi, Guijarro, J. Iñaki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3541406/
https://www.ncbi.nlm.nih.gov/pubmed/23326363
http://dx.doi.org/10.1371/journal.pone.0052908
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author Guillière, Florence
Danioux, Chloé
Jaubert, Carole
Desnoues, Nicole
Delepierre, Muriel
Prangishvili, David
Sezonov, Guennadi
Guijarro, J. Iñaki
author_facet Guillière, Florence
Danioux, Chloé
Jaubert, Carole
Desnoues, Nicole
Delepierre, Muriel
Prangishvili, David
Sezonov, Guennadi
Guijarro, J. Iñaki
author_sort Guillière, Florence
collection PubMed
description While the basal transcription machinery in archaea is eukaryal-like, transcription factors in archaea and their viruses are usually related to bacterial transcription factors. Nevertheless, some of these organisms show predicted classical zinc fingers motifs of the C2H2 type, which are almost exclusively found in proteins of eukaryotes and most often associated with transcription regulators. In this work, we focused on the protein AFV1p06 from the hyperthermophilic archaeal virus AFV1. The sequence of the protein consists of the classical eukaryotic C2H2 motif with the fourth histidine coordinating zinc missing, as well as of N- and C-terminal extensions. We showed that the protein AFV1p06 binds zinc and solved its solution structure by NMR. AFV1p06 displays a zinc finger fold with a novel structure extension and disordered N- and C-termini. Structure calculations show that a glutamic acid residue that coordinates zinc replaces the fourth histidine of the C2H2 motif. Electromobility gel shift assays indicate that the protein binds to DNA with different affinities depending on the DNA sequence. AFV1p06 is the first experimentally characterised archaeal zinc finger protein with a DNA binding activity. The AFV1p06 protein family has homologues in diverse viruses of hyperthermophilic archaea. A phylogenetic analysis points out a common origin of archaeal and eukaryotic C2H2 zinc fingers.
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spelling pubmed-35414062013-01-16 Solution Structure of an Archaeal DNA Binding Protein with an Eukaryotic Zinc Finger Fold Guillière, Florence Danioux, Chloé Jaubert, Carole Desnoues, Nicole Delepierre, Muriel Prangishvili, David Sezonov, Guennadi Guijarro, J. Iñaki PLoS One Research Article While the basal transcription machinery in archaea is eukaryal-like, transcription factors in archaea and their viruses are usually related to bacterial transcription factors. Nevertheless, some of these organisms show predicted classical zinc fingers motifs of the C2H2 type, which are almost exclusively found in proteins of eukaryotes and most often associated with transcription regulators. In this work, we focused on the protein AFV1p06 from the hyperthermophilic archaeal virus AFV1. The sequence of the protein consists of the classical eukaryotic C2H2 motif with the fourth histidine coordinating zinc missing, as well as of N- and C-terminal extensions. We showed that the protein AFV1p06 binds zinc and solved its solution structure by NMR. AFV1p06 displays a zinc finger fold with a novel structure extension and disordered N- and C-termini. Structure calculations show that a glutamic acid residue that coordinates zinc replaces the fourth histidine of the C2H2 motif. Electromobility gel shift assays indicate that the protein binds to DNA with different affinities depending on the DNA sequence. AFV1p06 is the first experimentally characterised archaeal zinc finger protein with a DNA binding activity. The AFV1p06 protein family has homologues in diverse viruses of hyperthermophilic archaea. A phylogenetic analysis points out a common origin of archaeal and eukaryotic C2H2 zinc fingers. Public Library of Science 2013-01-09 /pmc/articles/PMC3541406/ /pubmed/23326363 http://dx.doi.org/10.1371/journal.pone.0052908 Text en © 2013 Guillière et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Guillière, Florence
Danioux, Chloé
Jaubert, Carole
Desnoues, Nicole
Delepierre, Muriel
Prangishvili, David
Sezonov, Guennadi
Guijarro, J. Iñaki
Solution Structure of an Archaeal DNA Binding Protein with an Eukaryotic Zinc Finger Fold
title Solution Structure of an Archaeal DNA Binding Protein with an Eukaryotic Zinc Finger Fold
title_full Solution Structure of an Archaeal DNA Binding Protein with an Eukaryotic Zinc Finger Fold
title_fullStr Solution Structure of an Archaeal DNA Binding Protein with an Eukaryotic Zinc Finger Fold
title_full_unstemmed Solution Structure of an Archaeal DNA Binding Protein with an Eukaryotic Zinc Finger Fold
title_short Solution Structure of an Archaeal DNA Binding Protein with an Eukaryotic Zinc Finger Fold
title_sort solution structure of an archaeal dna binding protein with an eukaryotic zinc finger fold
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3541406/
https://www.ncbi.nlm.nih.gov/pubmed/23326363
http://dx.doi.org/10.1371/journal.pone.0052908
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