Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.

Nine human neurodegenerative diseases, including Huntington's disease and several spinocerebellar ataxia, are associated to the aggregation of proteins comprising an extended tract of consecutive glutamine residues (polyQs) once it exceeds a certain length threshold. This event is believed to b...

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Autores principales:	Matteo Ramazzotti, Elodie Monsellier, Choumouss Kamoun, Donatella Degl'Innocenti, Ronald Melki
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d637a89691874b8bafeff0e8fa609828
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spelling	oai:doaj.org-article:d637a89691874b8bafeff0e8fa6098282021-11-18T07:29:04ZPolyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.1932-620310.1371/journal.pone.0030824https://doaj.org/article/d637a89691874b8bafeff0e8fa6098282012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22312432/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Nine human neurodegenerative diseases, including Huntington's disease and several spinocerebellar ataxia, are associated to the aggregation of proteins comprising an extended tract of consecutive glutamine residues (polyQs) once it exceeds a certain length threshold. This event is believed to be the consequence of the expansion of polyCAG codons during the replication process. This is in apparent contradiction with the fact that many polyQs-containing proteins remain soluble and are encoded by invariant genes in a number of eukaryotes. The latter suggests that polyQs expansion and/or aggregation might be counter-selected through a genetic and/or protein context. To identify this context, we designed a software that scrutinize entire proteomes in search for imperfect polyQs. The nature of residues flanking the polyQs and that of residues other than Gln within polyQs (insertions) were assessed. We discovered strong amino acid residue biases robustly associated to polyQs in the 15 eukaryotic proteomes we examined, with an over-representation of Pro, Leu and His and an under-representation of Asp, Cys and Gly amino acid residues. These biases are conserved amongst unrelated proteins and are independent of specific functional classes. Our findings suggest that specific residues have been co-selected with polyQs during evolution. We discuss the possible selective pressures responsible of the observed biases.Matteo RamazzottiElodie MonsellierChoumouss KamounDonatella Degl'InnocentiRonald MelkiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 2, p e30824 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Matteo Ramazzotti Elodie Monsellier Choumouss Kamoun Donatella Degl'Innocenti Ronald Melki Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.
description	Nine human neurodegenerative diseases, including Huntington's disease and several spinocerebellar ataxia, are associated to the aggregation of proteins comprising an extended tract of consecutive glutamine residues (polyQs) once it exceeds a certain length threshold. This event is believed to be the consequence of the expansion of polyCAG codons during the replication process. This is in apparent contradiction with the fact that many polyQs-containing proteins remain soluble and are encoded by invariant genes in a number of eukaryotes. The latter suggests that polyQs expansion and/or aggregation might be counter-selected through a genetic and/or protein context. To identify this context, we designed a software that scrutinize entire proteomes in search for imperfect polyQs. The nature of residues flanking the polyQs and that of residues other than Gln within polyQs (insertions) were assessed. We discovered strong amino acid residue biases robustly associated to polyQs in the 15 eukaryotic proteomes we examined, with an over-representation of Pro, Leu and His and an under-representation of Asp, Cys and Gly amino acid residues. These biases are conserved amongst unrelated proteins and are independent of specific functional classes. Our findings suggest that specific residues have been co-selected with polyQs during evolution. We discuss the possible selective pressures responsible of the observed biases.
format	article
author	Matteo Ramazzotti Elodie Monsellier Choumouss Kamoun Donatella Degl'Innocenti Ronald Melki
author_facet	Matteo Ramazzotti Elodie Monsellier Choumouss Kamoun Donatella Degl'Innocenti Ronald Melki
author_sort	Matteo Ramazzotti
title	Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.
title_short	Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.
title_full	Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.
title_fullStr	Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.
title_full_unstemmed	Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.
title_sort	polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/d637a89691874b8bafeff0e8fa609828
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Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.

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