Enolases: storage compounds in seeds? Evidence from a proteomic comparison of zygotic and somatic embryos of Cyclamen persicum Mill.
Somatic embryogenesis is well established for the economic relevant ornamental crop Cyclamen and thus could supplement the elaborate propagation via seeds. However, the use of somatic embryogenesis for commercial large scale propagation is still limited due to physiological disorders and asynchronous development within emerged embryos. To overcome these problems, profound knowledge of the physiological processes in Cyclamen embryogenesis is essential. Thus, the proteomes of somatic and zygotic embryos were characterised in a comparative approach. Protein separation via two dimensional IEF-SDS PAGE led to a resolution of more than 1,000 protein spots/gel. Overall, 246 proteins were of differential abundance in the two tissues compared. Mass spectrometry analysis of the 300 most abundant protein spots resulted in the identification of 247 proteins, which represent 90 distinct protein species. Fifty-five percent of the 247 proteins belong to only three physiological categories: glycolysis, protein folding and stress response. The latter physiological process was especially predominant in the somatic embryos. Remarkably, the glycolytic enzyme enolase was the protein most frequently detected and thus is supposed to play an important role in Cyclamen embryogenesis. Data are presented that indicate involvement of "small enolases" as storage proteins in Cyclamen. A digital reference map was established via a novel software tool for the web-based presentation of proteome data linked to KEGG and ExPasy protein-databases and both were made publicly available online.
Institute of Plant Genetics, Leibniz Universitaet Hannover, Herrenhaeuser Str. 2, 30419 Hannover, Germany. rode@genetik.uni-hannover.de
Christina
C
Rode
Sébastien
S
Gallien
Dimitri
D
Heintz
Alain
A
Van Dorsselaer
Hans-Peter
HP
Braun
Traud
T
Winkelmann
D031824:Cyclamen / Q000737:chemistry* / Q000196:embryology / Q000201:enzymology* / Q000235:genetics; D015180:Electrophoresis, Gel, Two-Dimensional; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D010802:Phylogeny; D040901:Proteomics; D012639:Seeds / Q000737:chemistry / Q000201:enzymology; D015053:Zygote / Q000737:chemistry* / Q000201:enzymology*
D010751:Phosphopyruvate Hydratase
FEBS Lett. 2001 Mar 2;491(3):188-92
11240125
J Biol Chem. 1957 Jul;227(1):301-12
13449074
Plant Cell. 1991 Jul;3(7):719-35
1841726
Plant Cell. 2002;14 Suppl:S15-45
12045268
Plant Cell Rep. 2008 Feb;27(2):347-56
17874111
Proteomics. 2004 Aug;4(8):2437-47
15274138
Cell Mol Life Sci. 2004 Jan;61(2):192-208
14745498
Biochemistry. 1996 Apr 9;35(14):4349-58
8605183
J Cell Biol. 1988 Dec;107(6 Pt 2):2729-36
2462567
Proteomics. 2005 Feb;5(2):461-73
15627954
Plant Cell. 1995 Jul;7(7):1085-1097
12242399
Plant Physiol. 2006 May;141(1):32-46
16543413
Plant Physiol. 1986 Jul;81(3):802-6
16664906
Electrophoresis. 1990 Feb;11(2):101-17
1692528
Ann Bot. 2003 Jun;91(7):755-69
12730067
Plant Physiol. 2005 Apr;137(4):1397-419
15824287
Plant J. 2004 Sep;39(5):715-33
15315634
Planta. 2006 Aug;224(3):508-19
16496095
Biochem J. 1971 Feb;121(3):379-90
5154523
Plant Cell. 1993 Oct;5(10):1411-1423
12271037
New Phytol. 2010 Feb;185(3):649-62
20002588
J Exp Bot. 2009;60(6):1663-78
19286915
J Agric Food Chem. 1999 May;47(5):2168-72
10552514
Eur J Biochem. 2001 Oct;268(19):5037-44
11589694
Plant Physiol. 2007 Mar;143(3):1203-19
17237188
Proteomics. 2008 Oct;8(20):4214-25
18924179
Plant Mol Biol. 2004 May;55(1):109-20
15604668
BMC Plant Biol. 2010 Apr 28;10:77
20426818
Biol Rev Camb Philos Soc. 1995 Aug;70(3):375-426
7626727
Curr Opin Struct Biol. 1996 Dec;6(6):736-43
8994873
Adv Enzyme Regul. 1998;38:377-92
9762364
Biochem Soc Trans. 2000 Dec;28(6):779-81
11171206
J Proteome Res. 2007 Aug;6(8):3232-41
17580850