Brachypodium distachyon grain: identification and subcellular localization of storage proteins.
Seed storage proteins are of great importance in nutrition and in industrial transformation because of their functional properties. Brachypodium distachyon has been proposed as a new model plant to study temperate cereals. The protein composition of Brachypodium grain was investigated by separating the proteins on the basis of their solubility combined with a proteomic approach. Salt-soluble proteins as well as salt-insoluble proteins separated by two-dimensional gel electrophoresis revealed 284 and 120 spots, respectively. Proteins from the major spots were sequenced by mass spectrometry and identified by searching against a Brachypodium putative protein database. Our analysis detected globulins and prolamins but no albumins. Globulins were represented mainly by the 11S type and their solubility properties corresponded to the glutelin found in rice. An in silico search for storage proteins returned more translated genes than expressed products identified by mass spectrometry, particularly in the case of prolamin type proteins, reflecting a strong expression of globulins at the expense of prolamins. Microscopic examination of endosperm cells revealed scarce small-size starch granules surrounded by protein bodies containing 11S globulins. The presence of protein bodies containing glutelins makes B. distachyon closer to rice or oat than to wheat endosperm.
Larré
C
C
UR1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes, France. larre@nantes.inra.fr
Penninck
S
S
Bouchet
B
B
Lollier
V
V
Tranquet
O
O
Denery-Papini
S
S
Guillon
F
F
Rogniaux
H
H
D015180:Electrophoresis, Gel, Two-Dimensional; D005916:Globulins / Q000378:metabolism; D013058:Mass Spectrometry; D046529:Microscopy, Electron, Transmission; D010940:Plant Proteins / Q000378:metabolism*; D006109:Poaceae / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D055315:Prolamins / Q000378:metabolism; D012639:Seeds / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure
D005916:Globulins; D010940:Plant Proteins; D055315:Prolamins
Plant Physiol. 1986 Dec;82(4):1069-75
16665136
Biochem J. 2007 Jun 1;404(2):247-56
17313365
Plant Biotechnol J. 2008 Apr;6(3):236-45
18004984
Planta. 2007 Apr;225(5):1287-99
17086400
Ann Bot. 2007 Nov;100(5):941-50
17478546
Biochem Genet. 1989 Apr;27(3-4):239-51
2775172
Funct Integr Genomics. 2008 May;8(2):135-47
17985162
Eur J Biochem. 1991 Mar 28;196(3):617-21
2013284
Nucleic Acids Res. 1997 Sep 1;25(17):3389-402
9254694
Appl Spectrosc. 2008 Aug;62(8):895-900
18702863
Nature. 1970 Aug 15;227(5259):680-5
5432063
Plant Biotechnol J. 2008 Aug;6(6):529-59
18507792
Plant Physiol. 1991 Mar;95(3):973-5
16668082
Plant Physiol. 2001 Mar;125(3):1198-205
11244101
Plant Cell. 2002 Nov;14(11):2863-82
12417707
Plant Physiol. 2001 Jun;126(2):835-48
11402211
J Agric Food Chem. 2007 Jul 25;55(15):6074-81
17580876
Nature. 2010 Feb 11;463(7282):763-8
20148030
J Proteome Res. 2007 Apr;6(4):1342-53
17305382
J Nutr. 2005 May;135(5):1215-22
15867306
Mol Gen Genet. 1993 May;239(1-2):209-18
8510647
J Exp Bot. 2002 Apr;53(370):947-58
11912237
Plant Cell Rep. 2008 Mar;27(3):471-8
17999063
Biochem J. 1990 Apr 1;267(1):1-12
2183790
Trends Plant Sci. 2008 Apr;13(4):172-7
18343709
Plant Mol Biol. 2009 May;70(1-2):47-61
19184460
Proteomics. 2008 Apr;8(8):1692-705
18340629
Plant Cell. 1995 Jul;7(7):945-56
7640527
Nucleic Acids Res. 1985 Oct 25;13(20):7327-39
4059057
Theor Appl Genet. 2008 Aug;117(4):555-63
18528675
Theor Appl Genet. 2009 Nov;119(8):1397-412
19727653
Plant Cell. 1989 Apr;1(4):459-69
2562565
Int J Food Microbiol. 2003 Oct 15;87(1-2):63-73
12927708
Trends Biotechnol. 2006 Jul;24(7):305-11
16682090
Plant Physiol. 1988 Jul;87(3):698-704
16666210
Theor Appl Genet. 2006 Jul;113(2):186-95
16791686
BMC Plant Biol. 2009 Jul 17;9:93
19615078