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Biochem J. 2019 Mar 12;476(5):843-857. doi: 10.1042/BCJ20180911.

Dynamic hydrolase labelling as a marker for seed quality in Arabidopsis seeds.

Author information

1
Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.
2
Chemische Biologie, ZMB, Fakultät für Biologie, Universität Duisburg-Essen, 45117 Essen, Germany.
3
The Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford, U.K.
4
Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany jmisas@uni-koeln.de.
5
The Terrestrial Microbiology Lab, Botanical Institute, University of Cologne, 50674 Cologne, Germany.

Abstract

Seed quality is affected by different constituents of the seed. In general, seed lots are considered to be of high quality when they exhibit fast and homogeneous germination. When seeds are stored, they undergo different degrees of damage that have detrimental effects on their quality. Therefore, accurate prediction of the seed quality and viability levels of a seed lot is of high importance in the seed-producing industry. Here, we describe the use of activity-based protein profiling of proteases to evaluate the quality of artificially and naturally aged seeds of Arabidopsis thaliana Using this approach, we have identified two protease activities with opposite behaviours in aged seeds of Arabidopsis that correlate with the quality status of the seeds. We show that vacuolar processing enzymes (VPEs) become more active during the ageing process, in both artificial and natural ageing treatments. Secondly, we demonstrate that serine hydrolases are active at the beginning of our artificial ageing treatment, but their labelling decreases along with seed viability. We present a list of candidate hydrolases active during seed germination and propose that these protease activities can be used in combination with VPEs to develop novel markers of seed quality.

KEYWORDS:

ABPP; Arabidopsis thaliana; VPEs; protease activity; seed quality markers; serine hydrolases

PMID:
30782971
DOI:
10.1042/BCJ20180911

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