Proteomics reveals novel Drosophila seminal fluid proteins transferred at mating.

Across diverse taxa, seminal fluid proteins (Sfps) transferred at mating affect the reproductive success of both sexes. Such reproductive proteins often evolve under positive selection between species; because of this rapid divergence, Sfps are hypothesized to play a role in speciation by contributi...

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Autores principales:	Geoffrey D Findlay, Xianhua Yi, Michael J Maccoss, Willie J Swanson
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2008
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/3d7d07b87fb44cc48467559fd350442d
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spelling	oai:doaj.org-article:3d7d07b87fb44cc48467559fd350442d2021-11-25T05:33:16ZProteomics reveals novel Drosophila seminal fluid proteins transferred at mating.1544-91731545-788510.1371/journal.pbio.0060178https://doaj.org/article/3d7d07b87fb44cc48467559fd350442d2008-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18666829/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Across diverse taxa, seminal fluid proteins (Sfps) transferred at mating affect the reproductive success of both sexes. Such reproductive proteins often evolve under positive selection between species; because of this rapid divergence, Sfps are hypothesized to play a role in speciation by contributing to reproductive isolation between populations. In Drosophila, individual Sfps have been characterized and are known to alter male sperm competitive ability and female post-mating behavior, but a proteomic-scale view of the transferred Sfps has been missing. Here we describe a novel proteomic method that uses whole-organism isotopic labeling to detect transferred Sfps in mated female D. melanogaster. We identified 63 proteins, which were previously unknown to function in reproduction, and confirmed the transfer of dozens of predicted Sfps. Relative quantification of protein abundance revealed that several of these novel Sfps are abundant in seminal fluid. Positive selection and tandem gene duplication are the prevailing forces of Sfp evolution, and comparative proteomics with additional species revealed lineage-specific changes in seminal fluid content. We also report a proteomic-based gene discovery method that uncovered 19 previously unannotated genes in D. melanogaster. Our results demonstrate an experimental method to identify transferred proteins in any system that is amenable to isotopic labeling, and they underscore the power of combining proteomic and evolutionary analyses to shed light on the complex process of Drosophila reproduction.Geoffrey D FindlayXianhua YiMichael J MaccossWillie J SwansonPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 6, Iss 7, p e178 (2008)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Geoffrey D Findlay Xianhua Yi Michael J Maccoss Willie J Swanson Proteomics reveals novel Drosophila seminal fluid proteins transferred at mating.
description	Across diverse taxa, seminal fluid proteins (Sfps) transferred at mating affect the reproductive success of both sexes. Such reproductive proteins often evolve under positive selection between species; because of this rapid divergence, Sfps are hypothesized to play a role in speciation by contributing to reproductive isolation between populations. In Drosophila, individual Sfps have been characterized and are known to alter male sperm competitive ability and female post-mating behavior, but a proteomic-scale view of the transferred Sfps has been missing. Here we describe a novel proteomic method that uses whole-organism isotopic labeling to detect transferred Sfps in mated female D. melanogaster. We identified 63 proteins, which were previously unknown to function in reproduction, and confirmed the transfer of dozens of predicted Sfps. Relative quantification of protein abundance revealed that several of these novel Sfps are abundant in seminal fluid. Positive selection and tandem gene duplication are the prevailing forces of Sfp evolution, and comparative proteomics with additional species revealed lineage-specific changes in seminal fluid content. We also report a proteomic-based gene discovery method that uncovered 19 previously unannotated genes in D. melanogaster. Our results demonstrate an experimental method to identify transferred proteins in any system that is amenable to isotopic labeling, and they underscore the power of combining proteomic and evolutionary analyses to shed light on the complex process of Drosophila reproduction.
format	article
author	Geoffrey D Findlay Xianhua Yi Michael J Maccoss Willie J Swanson
author_facet	Geoffrey D Findlay Xianhua Yi Michael J Maccoss Willie J Swanson
author_sort	Geoffrey D Findlay
title	Proteomics reveals novel Drosophila seminal fluid proteins transferred at mating.
title_short	Proteomics reveals novel Drosophila seminal fluid proteins transferred at mating.
title_full	Proteomics reveals novel Drosophila seminal fluid proteins transferred at mating.
title_fullStr	Proteomics reveals novel Drosophila seminal fluid proteins transferred at mating.
title_full_unstemmed	Proteomics reveals novel Drosophila seminal fluid proteins transferred at mating.
title_sort	proteomics reveals novel drosophila seminal fluid proteins transferred at mating.
publisher	Public Library of Science (PLoS)
publishDate	2008
url	https://doaj.org/article/3d7d07b87fb44cc48467559fd350442d
work_keys_str_mv	AT geoffreydfindlay proteomicsrevealsnoveldrosophilaseminalfluidproteinstransferredatmating AT xianhuayi proteomicsrevealsnoveldrosophilaseminalfluidproteinstransferredatmating AT michaeljmaccoss proteomicsrevealsnoveldrosophilaseminalfluidproteinstransferredatmating AT williejswanson proteomicsrevealsnoveldrosophilaseminalfluidproteinstransferredatmating
_version_	1718414630631505920

Proteomics reveals novel Drosophila seminal fluid proteins transferred at mating.

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