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Comparative Proteomics of Rubber Latex Revealed Multiple Protein Species of REF/SRPP Family Respond Diversely to Ethylene Stimulation among Different Rubber Tree Clones

Rubber elongation factor (REF) and small rubber particle protein (SRPP) are two key factors for natural rubber biosynthesis. To further understand the roles of these proteins in rubber formation, six different genes for latex abundant REF or SRPP proteins, including REF(138,175,258) and SRPP(117,204...

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Autores principales: Tong, Zheng, Wang, Dan, Sun, Yong, Yang, Qian, Meng, Xueru, Wang, Limin, Feng, Weiqiang, Li, Ling, Wurtele, Eve Syrkin, Wang, Xuchu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5454871/
https://www.ncbi.nlm.nih.gov/pubmed/28468331
http://dx.doi.org/10.3390/ijms18050958
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author Tong, Zheng
Wang, Dan
Sun, Yong
Yang, Qian
Meng, Xueru
Wang, Limin
Feng, Weiqiang
Li, Ling
Wurtele, Eve Syrkin
Wang, Xuchu
author_facet Tong, Zheng
Wang, Dan
Sun, Yong
Yang, Qian
Meng, Xueru
Wang, Limin
Feng, Weiqiang
Li, Ling
Wurtele, Eve Syrkin
Wang, Xuchu
author_sort Tong, Zheng
collection PubMed
description Rubber elongation factor (REF) and small rubber particle protein (SRPP) are two key factors for natural rubber biosynthesis. To further understand the roles of these proteins in rubber formation, six different genes for latex abundant REF or SRPP proteins, including REF(138,175,258) and SRPP(117,204,243), were characterized from Hevea brasiliensis Reyan (RY) 7-33-97. Sequence analysis showed that REFs have a variable and long N-terminal, whereas SRPPs have a variable and long C-terminal beyond the REF domain, and REF(258) has a β subunit of ATPase in its N-terminal. Through two-dimensional electrophoresis (2-DE), each REF/SRPP protein was separated into multiple protein spots on 2-DE gels, indicating they have multiple protein species. The abundance of REF/SRPP proteins was compared between ethylene and control treatments or among rubber tree clones with different levels of latex productivity by analyzing 2-DE gels. The total abundance of each REF/SRPP protein decreased or changed a little upon ethylene stimulation, whereas the abundance of multiple protein species of the same REF/SRPP changed diversely. Among the three rubber tree clones, the abundance of the protein species also differed significantly. Especially, two protein species of REF(175) or REF(258) were ethylene-responsive only in the high latex productivity clone RY 8-79 instead of in RY 7-33-97 and PR 107. Some individual protein species were positively related to ethylene stimulation and latex productivity. These results suggested that the specific protein species could be more important than others for rubber production and post-translational modifications might play important roles in rubber biosynthesis.
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spelling pubmed-54548712017-06-08 Comparative Proteomics of Rubber Latex Revealed Multiple Protein Species of REF/SRPP Family Respond Diversely to Ethylene Stimulation among Different Rubber Tree Clones Tong, Zheng Wang, Dan Sun, Yong Yang, Qian Meng, Xueru Wang, Limin Feng, Weiqiang Li, Ling Wurtele, Eve Syrkin Wang, Xuchu Int J Mol Sci Article Rubber elongation factor (REF) and small rubber particle protein (SRPP) are two key factors for natural rubber biosynthesis. To further understand the roles of these proteins in rubber formation, six different genes for latex abundant REF or SRPP proteins, including REF(138,175,258) and SRPP(117,204,243), were characterized from Hevea brasiliensis Reyan (RY) 7-33-97. Sequence analysis showed that REFs have a variable and long N-terminal, whereas SRPPs have a variable and long C-terminal beyond the REF domain, and REF(258) has a β subunit of ATPase in its N-terminal. Through two-dimensional electrophoresis (2-DE), each REF/SRPP protein was separated into multiple protein spots on 2-DE gels, indicating they have multiple protein species. The abundance of REF/SRPP proteins was compared between ethylene and control treatments or among rubber tree clones with different levels of latex productivity by analyzing 2-DE gels. The total abundance of each REF/SRPP protein decreased or changed a little upon ethylene stimulation, whereas the abundance of multiple protein species of the same REF/SRPP changed diversely. Among the three rubber tree clones, the abundance of the protein species also differed significantly. Especially, two protein species of REF(175) or REF(258) were ethylene-responsive only in the high latex productivity clone RY 8-79 instead of in RY 7-33-97 and PR 107. Some individual protein species were positively related to ethylene stimulation and latex productivity. These results suggested that the specific protein species could be more important than others for rubber production and post-translational modifications might play important roles in rubber biosynthesis. MDPI 2017-05-02 /pmc/articles/PMC5454871/ /pubmed/28468331 http://dx.doi.org/10.3390/ijms18050958 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Tong, Zheng
Wang, Dan
Sun, Yong
Yang, Qian
Meng, Xueru
Wang, Limin
Feng, Weiqiang
Li, Ling
Wurtele, Eve Syrkin
Wang, Xuchu
Comparative Proteomics of Rubber Latex Revealed Multiple Protein Species of REF/SRPP Family Respond Diversely to Ethylene Stimulation among Different Rubber Tree Clones
title Comparative Proteomics of Rubber Latex Revealed Multiple Protein Species of REF/SRPP Family Respond Diversely to Ethylene Stimulation among Different Rubber Tree Clones
title_full Comparative Proteomics of Rubber Latex Revealed Multiple Protein Species of REF/SRPP Family Respond Diversely to Ethylene Stimulation among Different Rubber Tree Clones
title_fullStr Comparative Proteomics of Rubber Latex Revealed Multiple Protein Species of REF/SRPP Family Respond Diversely to Ethylene Stimulation among Different Rubber Tree Clones
title_full_unstemmed Comparative Proteomics of Rubber Latex Revealed Multiple Protein Species of REF/SRPP Family Respond Diversely to Ethylene Stimulation among Different Rubber Tree Clones
title_short Comparative Proteomics of Rubber Latex Revealed Multiple Protein Species of REF/SRPP Family Respond Diversely to Ethylene Stimulation among Different Rubber Tree Clones
title_sort comparative proteomics of rubber latex revealed multiple protein species of ref/srpp family respond diversely to ethylene stimulation among different rubber tree clones
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5454871/
https://www.ncbi.nlm.nih.gov/pubmed/28468331
http://dx.doi.org/10.3390/ijms18050958
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