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Natural variation in floral nectar proteins of two Nicotiana attenuata accessions
BACKGROUND: Floral nectar (FN) contains not only energy-rich compounds to attract pollinators, but also defense chemicals and several proteins. However, proteomic analysis of FN has been hampered by the lack of publically available sequence information from nectar-producing plants. Here we used next...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3728157/ https://www.ncbi.nlm.nih.gov/pubmed/23848992 http://dx.doi.org/10.1186/1471-2229-13-101 |
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author | Seo, Pil Joon Wielsch, Natalie Kessler, Danny Svatos, Ales Park, Chung-Mo Baldwin, Ian T Kim, Sang-Gyu |
author_facet | Seo, Pil Joon Wielsch, Natalie Kessler, Danny Svatos, Ales Park, Chung-Mo Baldwin, Ian T Kim, Sang-Gyu |
author_sort | Seo, Pil Joon |
collection | PubMed |
description | BACKGROUND: Floral nectar (FN) contains not only energy-rich compounds to attract pollinators, but also defense chemicals and several proteins. However, proteomic analysis of FN has been hampered by the lack of publically available sequence information from nectar-producing plants. Here we used next-generation sequencing and advanced proteomics to profile FN proteins in the opportunistic outcrossing wild tobacco, Nicotiana attenuata. RESULTS: We constructed a transcriptome database of N. attenuata and characterized its nectar proteome using LC-MS/MS. The FN proteins of N. attenuata included nectarins, sugar-cleaving enzymes (glucosidase, galactosidase, and xylosidase), RNases, pathogen-related proteins, and lipid transfer proteins. Natural variation in FN proteins of eleven N. attenuata accessions revealed a negative relationship between the accumulation of two abundant proteins, nectarin1b and nectarin5. In addition, microarray analysis of nectary tissues revealed that protein accumulation in FN is not simply correlated with the accumulation of transcripts encoding FN proteins and identified a group of genes that were specifically expressed in the nectary. CONCLUSIONS: Natural variation of identified FN proteins in the ecological model plant N. attenuata suggests that nectar chemistry may have a complex function in plant-pollinator-microbe interactions. |
format | Online Article Text |
id | pubmed-3728157 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-37281572013-07-31 Natural variation in floral nectar proteins of two Nicotiana attenuata accessions Seo, Pil Joon Wielsch, Natalie Kessler, Danny Svatos, Ales Park, Chung-Mo Baldwin, Ian T Kim, Sang-Gyu BMC Plant Biol Research Article BACKGROUND: Floral nectar (FN) contains not only energy-rich compounds to attract pollinators, but also defense chemicals and several proteins. However, proteomic analysis of FN has been hampered by the lack of publically available sequence information from nectar-producing plants. Here we used next-generation sequencing and advanced proteomics to profile FN proteins in the opportunistic outcrossing wild tobacco, Nicotiana attenuata. RESULTS: We constructed a transcriptome database of N. attenuata and characterized its nectar proteome using LC-MS/MS. The FN proteins of N. attenuata included nectarins, sugar-cleaving enzymes (glucosidase, galactosidase, and xylosidase), RNases, pathogen-related proteins, and lipid transfer proteins. Natural variation in FN proteins of eleven N. attenuata accessions revealed a negative relationship between the accumulation of two abundant proteins, nectarin1b and nectarin5. In addition, microarray analysis of nectary tissues revealed that protein accumulation in FN is not simply correlated with the accumulation of transcripts encoding FN proteins and identified a group of genes that were specifically expressed in the nectary. CONCLUSIONS: Natural variation of identified FN proteins in the ecological model plant N. attenuata suggests that nectar chemistry may have a complex function in plant-pollinator-microbe interactions. BioMed Central 2013-07-13 /pmc/articles/PMC3728157/ /pubmed/23848992 http://dx.doi.org/10.1186/1471-2229-13-101 Text en Copyright © 2013 Seo et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Seo, Pil Joon Wielsch, Natalie Kessler, Danny Svatos, Ales Park, Chung-Mo Baldwin, Ian T Kim, Sang-Gyu Natural variation in floral nectar proteins of two Nicotiana attenuata accessions |
title | Natural variation in floral nectar proteins of two Nicotiana attenuata accessions |
title_full | Natural variation in floral nectar proteins of two Nicotiana attenuata accessions |
title_fullStr | Natural variation in floral nectar proteins of two Nicotiana attenuata accessions |
title_full_unstemmed | Natural variation in floral nectar proteins of two Nicotiana attenuata accessions |
title_short | Natural variation in floral nectar proteins of two Nicotiana attenuata accessions |
title_sort | natural variation in floral nectar proteins of two nicotiana attenuata accessions |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3728157/ https://www.ncbi.nlm.nih.gov/pubmed/23848992 http://dx.doi.org/10.1186/1471-2229-13-101 |
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