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Proteomic analysis reveals differential accumulation of small heat shock proteins and late embryogenesis abundant proteins between ABA-deficient mutant vp5 seeds and wild-type Vp5 seeds in maize

Overview of attention for article published in Frontiers in Plant Science, January 2015
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Title
Proteomic analysis reveals differential accumulation of small heat shock proteins and late embryogenesis abundant proteins between ABA-deficient mutant vp5 seeds and wild-type Vp5 seeds in maize
Published in
Frontiers in Plant Science, January 2015
DOI 10.3389/fpls.2014.00801
Pubmed ID
Authors

Xiaolin Wu, Fangping Gong, Le Yang, Xiuli Hu, Fuju Tai, Wei Wang

Abstract

ABA is a major plant hormone that plays important roles during many phases of plant life cycle, including seed development, maturity and dormancy, and especially the acquisition of desiccation tolerance. Understanding of the molecular basis of ABA-mediated plant response to stress is of interest not only in basic research on plant adaptation but also in applied research on plant productivity. Maize mutant viviparous-5 (vp5), deficient in ABA biosynthesis in seeds, is a useful material for studying ABA-mediated response in maize. Due to carotenoid deficiency, vp5 endosperm is white, compared to yellow Vp5 endosperm. However, the background difference at proteome level between vp5 and Vp5 seeds is unclear. This study aimed to characterize proteome alterations of maize vp5 seeds and to identify ABA-dependent proteins during seed maturation. We compared the embryo and endosperm proteomes of vp5 and Vp5 seeds by gel-based proteomics. Up to 46 protein spots, most in embryos, were found to be differentially accumulated between vp5 and Vp5. The identified proteins included small heat shock proteins (sHSPs), late embryogenesis abundant (LEA) proteins, stress proteins, storage proteins and enzymes among others. However, EMB564, the most abundant LEA protein in maize embryo, accumulated in comparable levels between vp5 and Vp5 embryos, which contrasted to previously characterized, greatly lowered expression of emb564 mRNA in vp5 embryos. Moreover, LEA proteins and sHSPs displayed differential accumulations in vp5 embryos: six out of eight identified LEA proteins decreased while nine sHSPs increased in abundance. Finally, we discussed the possible causes of global proteome alterations, especially the observed differential accumulation of identified LEA proteins and sHSPs in vp5 embryos. The data derived from this study provides new insight into ABA-dependent proteins and ABA-mediated response during maize seed maturation.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 54 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Mexico 1 2%
Argentina 1 2%
Belgium 1 2%
South Africa 1 2%
Unknown 50 93%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 12 22%
Student > Master 11 20%
Researcher 10 19%
Professor 4 7%
Student > Doctoral Student 3 6%
Other 6 11%
Unknown 8 15%
Readers by discipline Count As %
Agricultural and Biological Sciences 32 59%
Biochemistry, Genetics and Molecular Biology 7 13%
Medicine and Dentistry 2 4%
Chemical Engineering 1 2%
Business, Management and Accounting 1 2%
Other 1 2%
Unknown 10 19%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 20 January 2015.
All research outputs
#22,759,802
of 25,374,917 outputs
Outputs from Frontiers in Plant Science
#19,714
of 24,598 outputs
Outputs of similar age
#308,017
of 359,955 outputs
Outputs of similar age from Frontiers in Plant Science
#178
of 225 outputs
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