Tracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.

<h4>Background</h4>Fungal mating types in self-incompatible Pezizomycotina are specified by one of two alternate sequences occupying the same locus on corresponding chromosomes. One sequence is characterized by a gene encoding an HMG protein, while the hallmark of the other is a gene enc...

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Autores principales: Tom Martin, Shun-Wen Lu, Herman van Tilbeurgh, Daniel R Ripoll, Christina Dixelius, B Gillian Turgeon, Robert Debuchy
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spelling oai:doaj.org-article:1442b975d4c84ffaab91193e132580272021-11-18T07:01:57ZTracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.1932-620310.1371/journal.pone.0015199https://doaj.org/article/1442b975d4c84ffaab91193e132580272010-12-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21170349/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Fungal mating types in self-incompatible Pezizomycotina are specified by one of two alternate sequences occupying the same locus on corresponding chromosomes. One sequence is characterized by a gene encoding an HMG protein, while the hallmark of the other is a gene encoding a protein with an α1 domain showing similarity to the Matα1p protein of Saccharomyces cerevisiae. DNA-binding HMG proteins are ubiquitous and well characterized. In contrast, α1 domain proteins have limited distribution and their evolutionary origin is obscure, precluding a complete understanding of mating-type evolution in Ascomycota. Although much work has focused on the role of the S. cerevisiae Matα1p protein as a transcription factor, it has not yet been placed in any of the large families of sequence-specific DNA-binding proteins.<h4>Methodology/principal findings</h4>We present sequence comparisons, phylogenetic analyses, and in silico predictions of secondary and tertiary structures, which support our hypothesis that the α1 domain is related to the HMG domain. We have also characterized a new conserved motif in α1 proteins of Pezizomycotina. This motif is immediately adjacent to and downstream of the α1 domain and consists of a core sequence Y-[LMIF]-x(3)-G-[WL] embedded in a larger conserved motif.<h4>Conclusions/significance</h4>Our data suggest that extant α1-box genes originated from an ancestral HMG gene, which confirms the current model of mating-type evolution within the fungal kingdom. We propose to incorporate α1 proteins in a new subclass of HMG proteins termed MATα_HMG.Tom MartinShun-Wen LuHerman van TilbeurghDaniel R RipollChristina DixeliusB Gillian TurgeonRobert DebuchyPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 12, p e15199 (2010)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Tom Martin
Shun-Wen Lu
Herman van Tilbeurgh
Daniel R Ripoll
Christina Dixelius
B Gillian Turgeon
Robert Debuchy
Tracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.
description <h4>Background</h4>Fungal mating types in self-incompatible Pezizomycotina are specified by one of two alternate sequences occupying the same locus on corresponding chromosomes. One sequence is characterized by a gene encoding an HMG protein, while the hallmark of the other is a gene encoding a protein with an α1 domain showing similarity to the Matα1p protein of Saccharomyces cerevisiae. DNA-binding HMG proteins are ubiquitous and well characterized. In contrast, α1 domain proteins have limited distribution and their evolutionary origin is obscure, precluding a complete understanding of mating-type evolution in Ascomycota. Although much work has focused on the role of the S. cerevisiae Matα1p protein as a transcription factor, it has not yet been placed in any of the large families of sequence-specific DNA-binding proteins.<h4>Methodology/principal findings</h4>We present sequence comparisons, phylogenetic analyses, and in silico predictions of secondary and tertiary structures, which support our hypothesis that the α1 domain is related to the HMG domain. We have also characterized a new conserved motif in α1 proteins of Pezizomycotina. This motif is immediately adjacent to and downstream of the α1 domain and consists of a core sequence Y-[LMIF]-x(3)-G-[WL] embedded in a larger conserved motif.<h4>Conclusions/significance</h4>Our data suggest that extant α1-box genes originated from an ancestral HMG gene, which confirms the current model of mating-type evolution within the fungal kingdom. We propose to incorporate α1 proteins in a new subclass of HMG proteins termed MATα_HMG.
format article
author Tom Martin
Shun-Wen Lu
Herman van Tilbeurgh
Daniel R Ripoll
Christina Dixelius
B Gillian Turgeon
Robert Debuchy
author_facet Tom Martin
Shun-Wen Lu
Herman van Tilbeurgh
Daniel R Ripoll
Christina Dixelius
B Gillian Turgeon
Robert Debuchy
author_sort Tom Martin
title Tracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.
title_short Tracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.
title_full Tracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.
title_fullStr Tracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.
title_full_unstemmed Tracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.
title_sort tracing the origin of the fungal α1 domain places its ancestor in the hmg-box superfamily: implication for fungal mating-type evolution.
publisher Public Library of Science (PLoS)
publishDate 2010
url https://doaj.org/article/1442b975d4c84ffaab91193e13258027
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