Details
| Original language | English |
|---|---|
| Pages (from-to) | 508-519 |
| Number of pages | 12 |
| Journal | PLANTA |
| Volume | 224 |
| Issue number | 3 |
| Publication status | Published - 22 Feb 2006 |
Abstract
In the horticulturally important ornamental species Cyclamen persicum Mill., somatic embryogenesis is an efficient vegetative propagation method and the development of artificial seeds is an ultimate aim. This study aims at a systematic comparison of the proteomes of zygotic embryos, somatic embryos grown in liquid medium containing 30 or 60 g l-1 sucrose, germinating embryos of both types and endosperm in order to obtain novel insights into seed and germination physiology. Using high resolution two-dimensional isoelectric focussing/sodium dodecylsulfate polyacrylamide gel electrophoresis (2D IEF/SDS PAGE), 74% of the proteins expressed in zygotic embryos were found in similar abundance in somatic embryos grown in 60 g l-1 sucrose. Somatic embryos grown in 30 g l-1 sucrose accumulated fewer protein species than those grown in 60 g l-1. Selected proteins were identified following mass spectrometry (nano-LC-MS/MS). Four enzymes involved in glycolysis (UDP-glucose pyrophosphorylase, fructose bisphosphate aldolase, triosephosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase GAPDH) were specifically induced in somatic embryos. 11S globulin proteins identified by MS were present in high levels in somatic embryos, zygotic embryos and endosperm, whereas 7S globulins were detected mainly in endosperm and zygotic embryos. These are the first storage proteins identified in C. persicum. Xyloglucans are known to be another group of seed storage compounds in C. persicum. Interestingly, xyloglucan endotransglycosylases were found to be highly expressed in endosperm tissue. We discuss the physiological implications of these observations.
Keywords
- Endosperm, Mass spectrometry, Ornamental plant, Storage proteins, Two-dimensional polyacrylamide gel electrophoresis, Xyloglucan endotransglycosylase
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Agricultural and Biological Sciences(all)
- Plant Science
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In: PLANTA, Vol. 224, No. 3, 22.02.2006, p. 508-519.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Proteomic analyses of somatic and zygotic embryos of Cyclamen persicum Mill. reveal new insights into seed and germination physiology
AU - Winkelmann, Traud
AU - Heintz, Dimitri
AU - Van Dorsselaer, Alain
AU - Serek, Margrethe
AU - Braun, Hans Peter
PY - 2006/2/22
Y1 - 2006/2/22
N2 - In the horticulturally important ornamental species Cyclamen persicum Mill., somatic embryogenesis is an efficient vegetative propagation method and the development of artificial seeds is an ultimate aim. This study aims at a systematic comparison of the proteomes of zygotic embryos, somatic embryos grown in liquid medium containing 30 or 60 g l-1 sucrose, germinating embryos of both types and endosperm in order to obtain novel insights into seed and germination physiology. Using high resolution two-dimensional isoelectric focussing/sodium dodecylsulfate polyacrylamide gel electrophoresis (2D IEF/SDS PAGE), 74% of the proteins expressed in zygotic embryos were found in similar abundance in somatic embryos grown in 60 g l-1 sucrose. Somatic embryos grown in 30 g l-1 sucrose accumulated fewer protein species than those grown in 60 g l-1. Selected proteins were identified following mass spectrometry (nano-LC-MS/MS). Four enzymes involved in glycolysis (UDP-glucose pyrophosphorylase, fructose bisphosphate aldolase, triosephosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase GAPDH) were specifically induced in somatic embryos. 11S globulin proteins identified by MS were present in high levels in somatic embryos, zygotic embryos and endosperm, whereas 7S globulins were detected mainly in endosperm and zygotic embryos. These are the first storage proteins identified in C. persicum. Xyloglucans are known to be another group of seed storage compounds in C. persicum. Interestingly, xyloglucan endotransglycosylases were found to be highly expressed in endosperm tissue. We discuss the physiological implications of these observations.
AB - In the horticulturally important ornamental species Cyclamen persicum Mill., somatic embryogenesis is an efficient vegetative propagation method and the development of artificial seeds is an ultimate aim. This study aims at a systematic comparison of the proteomes of zygotic embryos, somatic embryos grown in liquid medium containing 30 or 60 g l-1 sucrose, germinating embryos of both types and endosperm in order to obtain novel insights into seed and germination physiology. Using high resolution two-dimensional isoelectric focussing/sodium dodecylsulfate polyacrylamide gel electrophoresis (2D IEF/SDS PAGE), 74% of the proteins expressed in zygotic embryos were found in similar abundance in somatic embryos grown in 60 g l-1 sucrose. Somatic embryos grown in 30 g l-1 sucrose accumulated fewer protein species than those grown in 60 g l-1. Selected proteins were identified following mass spectrometry (nano-LC-MS/MS). Four enzymes involved in glycolysis (UDP-glucose pyrophosphorylase, fructose bisphosphate aldolase, triosephosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase GAPDH) were specifically induced in somatic embryos. 11S globulin proteins identified by MS were present in high levels in somatic embryos, zygotic embryos and endosperm, whereas 7S globulins were detected mainly in endosperm and zygotic embryos. These are the first storage proteins identified in C. persicum. Xyloglucans are known to be another group of seed storage compounds in C. persicum. Interestingly, xyloglucan endotransglycosylases were found to be highly expressed in endosperm tissue. We discuss the physiological implications of these observations.
KW - Endosperm
KW - Mass spectrometry
KW - Ornamental plant
KW - Storage proteins
KW - Two-dimensional polyacrylamide gel electrophoresis
KW - Xyloglucan endotransglycosylase
UR - http://www.scopus.com/inward/record.url?scp=33746903924&partnerID=8YFLogxK
U2 - 10.1007/s00425-006-0238-8
DO - 10.1007/s00425-006-0238-8
M3 - Article
C2 - 16496095
AN - SCOPUS:33746903924
VL - 224
SP - 508
EP - 519
JO - PLANTA
JF - PLANTA
SN - 0032-0935
IS - 3
ER -