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Evolution of the vertebrate goose-type lysozyme gene family
BACKGROUND: Lysozyme g is an antibacterial enzyme that was first found in the eggs of some birds, but recently has been found in additional species, including non-vertebrates. Some previously characterized lysozyme g sequences are suggested to have altered secretion potential and enzymatic activity,...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4243810/ https://www.ncbi.nlm.nih.gov/pubmed/25167808 http://dx.doi.org/10.1186/s12862-014-0188-x |
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author | Irwin, David M |
author_facet | Irwin, David M |
author_sort | Irwin, David M |
collection | PubMed |
description | BACKGROUND: Lysozyme g is an antibacterial enzyme that was first found in the eggs of some birds, but recently has been found in additional species, including non-vertebrates. Some previously characterized lysozyme g sequences are suggested to have altered secretion potential and enzymatic activity, however the distribution of these altered sequences is unknown. Duplicated copies of the lysozyme g gene exist in some species; however, the origins of the duplicates and their roles in altered function are unclear. RESULTS: We identified 234 lysozyme g sequences from 118 vertebrate species, including 181 sequences that are full or near full length representing all vertebrate classes except cartilaginous fish. Phylogenetic analysis shows that most lysozyme g gene duplicates are recent or lineage specific events, however three amplification events are more ancient, those in an early amniote, an early mammal, and an early teleost. The older gene duplications are associated with changes in function, including changes in secretion potential and muramidase antibacterial enzymatic activity. CONCLUSIONS: Lysozyme g is an essential muramidase enzyme that is widespread in vertebrates. Duplication of the lysozyme g gene, and the retention of non-secreted isozymes that have lost enzymatic activity indicate that lysozyme g has an activity other than the muramidase activity associated with being an antibacterial enzyme. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12862-014-0188-x) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4243810 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-42438102014-11-26 Evolution of the vertebrate goose-type lysozyme gene family Irwin, David M BMC Evol Biol Research Article BACKGROUND: Lysozyme g is an antibacterial enzyme that was first found in the eggs of some birds, but recently has been found in additional species, including non-vertebrates. Some previously characterized lysozyme g sequences are suggested to have altered secretion potential and enzymatic activity, however the distribution of these altered sequences is unknown. Duplicated copies of the lysozyme g gene exist in some species; however, the origins of the duplicates and their roles in altered function are unclear. RESULTS: We identified 234 lysozyme g sequences from 118 vertebrate species, including 181 sequences that are full or near full length representing all vertebrate classes except cartilaginous fish. Phylogenetic analysis shows that most lysozyme g gene duplicates are recent or lineage specific events, however three amplification events are more ancient, those in an early amniote, an early mammal, and an early teleost. The older gene duplications are associated with changes in function, including changes in secretion potential and muramidase antibacterial enzymatic activity. CONCLUSIONS: Lysozyme g is an essential muramidase enzyme that is widespread in vertebrates. Duplication of the lysozyme g gene, and the retention of non-secreted isozymes that have lost enzymatic activity indicate that lysozyme g has an activity other than the muramidase activity associated with being an antibacterial enzyme. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12862-014-0188-x) contains supplementary material, which is available to authorized users. BioMed Central 2014-08-29 /pmc/articles/PMC4243810/ /pubmed/25167808 http://dx.doi.org/10.1186/s12862-014-0188-x Text en © Irwin; licensee BioMed Central Ltd 2014 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Irwin, David M Evolution of the vertebrate goose-type lysozyme gene family |
title | Evolution of the vertebrate goose-type lysozyme gene family |
title_full | Evolution of the vertebrate goose-type lysozyme gene family |
title_fullStr | Evolution of the vertebrate goose-type lysozyme gene family |
title_full_unstemmed | Evolution of the vertebrate goose-type lysozyme gene family |
title_short | Evolution of the vertebrate goose-type lysozyme gene family |
title_sort | evolution of the vertebrate goose-type lysozyme gene family |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4243810/ https://www.ncbi.nlm.nih.gov/pubmed/25167808 http://dx.doi.org/10.1186/s12862-014-0188-x |
work_keys_str_mv | AT irwindavidm evolutionofthevertebrategoosetypelysozymegenefamily |