Adaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.

A series of duplication events led to an expansion of clade B Serine Protease Inhibitors (SERPIN), currently displaying a large repertoire of functions in vertebrates. Accordingly, the recent duplicates SERPINB3 and B4 located in human 18q21.3 SERPIN cluster control the activity of different cystein...

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Autores principales:	Sílvia Gomes, Patrícia I Marques, Rune Matthiesen, Susana Seixas
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b8db2c91f1e64b98a47225307368aa18
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spelling	oai:doaj.org-article:b8db2c91f1e64b98a47225307368aa182021-11-25T06:04:15ZAdaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.1932-620310.1371/journal.pone.0104935https://doaj.org/article/b8db2c91f1e64b98a47225307368aa182014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25133778/?tool=EBIhttps://doaj.org/toc/1932-6203A series of duplication events led to an expansion of clade B Serine Protease Inhibitors (SERPIN), currently displaying a large repertoire of functions in vertebrates. Accordingly, the recent duplicates SERPINB3 and B4 located in human 18q21.3 SERPIN cluster control the activity of different cysteine and serine proteases, respectively. Here, we aim to assess SERPINB3 and B4 coevolution with their target proteases in order to understand the evolutionary forces shaping the accelerated divergence of these duplicates. Phylogenetic analysis of primate sequences placed the duplication event in a Hominoidae ancestor (∼30 Mya) and the emergence of SERPINB3 in Homininae (∼9 Mya). We detected evidence of strong positive selection throughout SERPINB4/B3 primate tree and target proteases, cathepsin L2 (CTSL2) and G (CTSG) and chymase (CMA1). Specifically, in the Homininae clade a perfect match was observed between the adaptive evolution of SERPINB3 and cathepsin S (CTSS) and most of sites under positive selection were located at the inhibitor/protease interface. Altogether our results seem to favour a coevolution hypothesis for SERPINB3, CTSS and CTSL2 and for SERPINB4 and CTSG and CMA1. A scenario of an accelerated evolution driven by host-pathogen interactions is also possible since SERPINB3/B4 are potent inhibitors of exogenous proteases, released by infectious agents. Finally, similar patterns of expression and the sharing of many regulatory motifs suggest neofunctionalization as the best fitted model of the functional divergence of SERPINB3 and B4 duplicates.Sílvia GomesPatrícia I MarquesRune MatthiesenSusana SeixasPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 8, p e104935 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sílvia Gomes Patrícia I Marques Rune Matthiesen Susana Seixas Adaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.
description	A series of duplication events led to an expansion of clade B Serine Protease Inhibitors (SERPIN), currently displaying a large repertoire of functions in vertebrates. Accordingly, the recent duplicates SERPINB3 and B4 located in human 18q21.3 SERPIN cluster control the activity of different cysteine and serine proteases, respectively. Here, we aim to assess SERPINB3 and B4 coevolution with their target proteases in order to understand the evolutionary forces shaping the accelerated divergence of these duplicates. Phylogenetic analysis of primate sequences placed the duplication event in a Hominoidae ancestor (∼30 Mya) and the emergence of SERPINB3 in Homininae (∼9 Mya). We detected evidence of strong positive selection throughout SERPINB4/B3 primate tree and target proteases, cathepsin L2 (CTSL2) and G (CTSG) and chymase (CMA1). Specifically, in the Homininae clade a perfect match was observed between the adaptive evolution of SERPINB3 and cathepsin S (CTSS) and most of sites under positive selection were located at the inhibitor/protease interface. Altogether our results seem to favour a coevolution hypothesis for SERPINB3, CTSS and CTSL2 and for SERPINB4 and CTSG and CMA1. A scenario of an accelerated evolution driven by host-pathogen interactions is also possible since SERPINB3/B4 are potent inhibitors of exogenous proteases, released by infectious agents. Finally, similar patterns of expression and the sharing of many regulatory motifs suggest neofunctionalization as the best fitted model of the functional divergence of SERPINB3 and B4 duplicates.
format	article
author	Sílvia Gomes Patrícia I Marques Rune Matthiesen Susana Seixas
author_facet	Sílvia Gomes Patrícia I Marques Rune Matthiesen Susana Seixas
author_sort	Sílvia Gomes
title	Adaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.
title_short	Adaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.
title_full	Adaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.
title_fullStr	Adaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.
title_full_unstemmed	Adaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.
title_sort	adaptive evolution and divergence of serpinb3: a young duplicate in great apes.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/b8db2c91f1e64b98a47225307368aa18
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Adaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.

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