Cargando…

Quantitative Proteomics Reveals that GmENO2 Proteins Are Involved in Response to Phosphate Starvation in the Leaves of Glycine max L.

Soybean (Glycine max L.) is a major crop providing important source for protein and oil for human life. Low phosphate (LP) availability is a critical limiting factor affecting soybean production. Soybean plants develop a series of strategies to adapt to phosphate (Pi) limitation condition. However,...

Descripción completa

Detalles Bibliográficos
Autores principales: Cheng, Ling, Min, Wanling, Li, Man, Zhou, Lili, Hsu, Chuan-Chih, Yang, Xuelian, Jiang, Xue, Ruan, Zhijie, Zhong, Yongjia, Wang, Zhi-Yong, Wang, Wenfei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7831476/
https://www.ncbi.nlm.nih.gov/pubmed/33477636
http://dx.doi.org/10.3390/ijms22020920
_version_ 1783641630656430080
author Cheng, Ling
Min, Wanling
Li, Man
Zhou, Lili
Hsu, Chuan-Chih
Yang, Xuelian
Jiang, Xue
Ruan, Zhijie
Zhong, Yongjia
Wang, Zhi-Yong
Wang, Wenfei
author_facet Cheng, Ling
Min, Wanling
Li, Man
Zhou, Lili
Hsu, Chuan-Chih
Yang, Xuelian
Jiang, Xue
Ruan, Zhijie
Zhong, Yongjia
Wang, Zhi-Yong
Wang, Wenfei
author_sort Cheng, Ling
collection PubMed
description Soybean (Glycine max L.) is a major crop providing important source for protein and oil for human life. Low phosphate (LP) availability is a critical limiting factor affecting soybean production. Soybean plants develop a series of strategies to adapt to phosphate (Pi) limitation condition. However, the underlying molecular mechanisms responsible for LP stress response remain largely unknown. Here, we performed a label-free quantification (LFQ) analysis of soybean leaves grown under low and high phosphate conditions. We identified 267 induced and 440 reduced differential proteins from phosphate-starved leaves. Almost a quarter of the LP decreased proteins are involved in translation processes, while the LP increased proteins are accumulated in chlorophyll biosynthetic and carbon metabolic processes. Among these induced proteins, an enolase protein, GmENO2a was found to be mostly induced protein. On the transcriptional level, GmENO2a and GmENO2b, but not GmENO2c or GmENO2d, were dramatically induced by phosphate starvation. Among 14 enolase genes, only GmENO2a and GmENO2b genes contain the P1BS motif in their promoter regions. Furthermore, GmENO2b was specifically induced in the GmPHR31 overexpressing soybean plants. Our findings provide molecular insights into how soybean plants tune basic carbon metabolic pathway to adapt to Pi deprivation through the ENO2 enzymes.
format Online
Article
Text
id pubmed-7831476
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-78314762021-01-26 Quantitative Proteomics Reveals that GmENO2 Proteins Are Involved in Response to Phosphate Starvation in the Leaves of Glycine max L. Cheng, Ling Min, Wanling Li, Man Zhou, Lili Hsu, Chuan-Chih Yang, Xuelian Jiang, Xue Ruan, Zhijie Zhong, Yongjia Wang, Zhi-Yong Wang, Wenfei Int J Mol Sci Article Soybean (Glycine max L.) is a major crop providing important source for protein and oil for human life. Low phosphate (LP) availability is a critical limiting factor affecting soybean production. Soybean plants develop a series of strategies to adapt to phosphate (Pi) limitation condition. However, the underlying molecular mechanisms responsible for LP stress response remain largely unknown. Here, we performed a label-free quantification (LFQ) analysis of soybean leaves grown under low and high phosphate conditions. We identified 267 induced and 440 reduced differential proteins from phosphate-starved leaves. Almost a quarter of the LP decreased proteins are involved in translation processes, while the LP increased proteins are accumulated in chlorophyll biosynthetic and carbon metabolic processes. Among these induced proteins, an enolase protein, GmENO2a was found to be mostly induced protein. On the transcriptional level, GmENO2a and GmENO2b, but not GmENO2c or GmENO2d, were dramatically induced by phosphate starvation. Among 14 enolase genes, only GmENO2a and GmENO2b genes contain the P1BS motif in their promoter regions. Furthermore, GmENO2b was specifically induced in the GmPHR31 overexpressing soybean plants. Our findings provide molecular insights into how soybean plants tune basic carbon metabolic pathway to adapt to Pi deprivation through the ENO2 enzymes. MDPI 2021-01-18 /pmc/articles/PMC7831476/ /pubmed/33477636 http://dx.doi.org/10.3390/ijms22020920 Text en © 2021 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
Cheng, Ling
Min, Wanling
Li, Man
Zhou, Lili
Hsu, Chuan-Chih
Yang, Xuelian
Jiang, Xue
Ruan, Zhijie
Zhong, Yongjia
Wang, Zhi-Yong
Wang, Wenfei
Quantitative Proteomics Reveals that GmENO2 Proteins Are Involved in Response to Phosphate Starvation in the Leaves of Glycine max L.
title Quantitative Proteomics Reveals that GmENO2 Proteins Are Involved in Response to Phosphate Starvation in the Leaves of Glycine max L.
title_full Quantitative Proteomics Reveals that GmENO2 Proteins Are Involved in Response to Phosphate Starvation in the Leaves of Glycine max L.
title_fullStr Quantitative Proteomics Reveals that GmENO2 Proteins Are Involved in Response to Phosphate Starvation in the Leaves of Glycine max L.
title_full_unstemmed Quantitative Proteomics Reveals that GmENO2 Proteins Are Involved in Response to Phosphate Starvation in the Leaves of Glycine max L.
title_short Quantitative Proteomics Reveals that GmENO2 Proteins Are Involved in Response to Phosphate Starvation in the Leaves of Glycine max L.
title_sort quantitative proteomics reveals that gmeno2 proteins are involved in response to phosphate starvation in the leaves of glycine max l.
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7831476/
https://www.ncbi.nlm.nih.gov/pubmed/33477636
http://dx.doi.org/10.3390/ijms22020920
work_keys_str_mv AT chengling quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT minwanling quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT liman quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT zhoulili quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT hsuchuanchih quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT yangxuelian quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT jiangxue quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT ruanzhijie quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT zhongyongjia quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT wangzhiyong quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl
AT wangwenfei quantitativeproteomicsrevealsthatgmeno2proteinsareinvolvedinresponsetophosphatestarvationintheleavesofglycinemaxl