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231223s2011 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erq334
|2 doi
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|a pubmed24n1337.xml
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|a (NLM)20974739
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Goggin, Danica E
|e verfasserin
|4 aut
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|a Selection for low or high primary dormancy in Lolium rigidum Gaud seeds results in constitutive differences in stress protein expression and peroxidase activity
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|c 2011
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 25.04.2011
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|a Date Revised 20.03.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Seed dormancy in wild Lolium rigidum Gaud (annual ryegrass) populations is highly variable and not well characterized at the biochemical level. To identify some of the determinants of dormancy level in these seeds, the proteomes of subpopulations selected for low and high levels of primary dormancy were compared by two-dimensional polyacrylamide gel electrophoresis of extracts from mature, dry seeds. High-dormancy seeds showed higher expression of small heat shock proteins, enolase, and glyoxalase I than the low-dormancy seeds. The functional relevance of these differences in protein expression was confirmed by the fact that high-dormancy seeds were more tolerant to high temperatures imposed at imbibition and had consistently higher glyoxalase I activity over 0-42 d dark stratification. Higher expression of a putative glutathione peroxidase in low-dormancy seeds was not accompanied by higher activity, but these seeds had a slightly more oxidized glutathione pool and higher total peroxidase activity. Overall, these biochemical and physiological differences suggest that L. rigidum seeds selected for low dormancy are more prepared for rapid germination via peroxidase-mediated cell wall weakening, whilst seeds selected for high dormancy are constitutively prepared to survive environmental stresses, even in the absence of stress during seed development
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Heat-Shock Proteins
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Peroxidase
|2 NLM
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|a EC 1.11.1.7
|2 NLM
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|a Powles, Stephen B
|e verfasserin
|4 aut
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|a Steadman, Kathryn J
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 62(2011), 3 vom: 20. Jan., Seite 1037-47
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:62
|g year:2011
|g number:3
|g day:20
|g month:01
|g pages:1037-47
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|u http://dx.doi.org/10.1093/jxb/erq334
|3 Volltext
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