Next Article in Journal
The Beneficial Effects of Allicin in Chronic Kidney Disease Are Comparable to Losartan
Previous Article in Journal
Lactoferrin: A Natural Glycoprotein Involved in Iron and Inflammatory Homeostasis
Article Menu
Issue 9 (September) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2017, 18(9), 1984; doi:10.3390/ijms18091984

iTRAQ-Based Quantitative Proteomic Analysis Reveals Cold Responsive Proteins Involved in Leaf Senescence in Upland Cotton (Gossypium hirsutum L.)

1
State Key Laboratory of Cotton Biology, Institute of Cotton Research of CAAS, Anyang 455000, China
2
College of Life Sciences, Key laboratory of Agrobiotechnology, Shihezi University, Shihezi 832003, China
*
Authors to whom correspondence should be addressed.
Received: 19 August 2017 / Revised: 8 September 2017 / Accepted: 11 September 2017 / Published: 16 September 2017
(This article belongs to the Section Molecular Botany)
View Full-Text   |   Download PDF [5265 KB, uploaded 16 September 2017]   |  

Abstract

Premature leaf senescence occurs in the ultimate phase of the plant, and it occurs through a complex series of actions regulated by stress, hormones and genes. In this study, a proteomic analysis was performed to analyze the factors that could induce premature leaf senescence in two cotton cultivars. We successfully identified 443 differential abundant proteins (DAPs) from 7388 high-confidence proteins at four stages between non-premature senescence (NS) and premature senescence (PS), among which 158 proteins were over-accumulated, 238 proteins were down-accumulated at four stages, and 47 proteins displayed overlapped accumulation. All the DAPs were mapped onto 21 different categories on the basis of a Clusters of Orthologous Groups (COG) analysis, and 9 clusters were based on accumulation. Gene Ontology (GO) enrichment results show that processes related to stress responses, including responses to cold temperatures and responses to hormones, are significantly differentially accumulated. More importantly, the enriched proteins were mapped in The Arabidopsis Information Resource (TAIR), showing that 58 proteins play an active role in abiotic stress, hormone signaling and leaf senescence. Among these proteins, 26 cold-responsive proteins (CRPs) are significantly differentially accumulated. The meteorological data showed that the median temperatures declined at approximately 15 days before the onset of aging, suggesting that a decrease in temperature is tightly linked to an onset of cotton leaf senescence. Because accumulations of H2O2 and increased jasmonic acid (JA) were detected during PS, we speculate that two pathways associated with JA and H2O2 are closely related to premature leaf senescence in cotton. View Full-Text
Keywords: premature leaf senescence; iTRAQ; cold-responsive proteins; proteomic; jasmonic acid premature leaf senescence; iTRAQ; cold-responsive proteins; proteomic; jasmonic acid
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Zheng, X.; Fan, S.; Wei, H.; Tao, C.; Ma, Q.; Ma, Q.; Zhang, S.; Li, H.; Pang, C.; Yu, S. iTRAQ-Based Quantitative Proteomic Analysis Reveals Cold Responsive Proteins Involved in Leaf Senescence in Upland Cotton (Gossypium hirsutum L.). Int. J. Mol. Sci. 2017, 18, 1984.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top