title: The endoplasmic reticulum stress induced by highly expressed OsrAAT reduces seed size via pre-mature programmed cell death.
abstract: The high accumulation of a recombinant protein in rice endosperm causes endoplasmic reticulum (ER) stress and in turn dramatically affects endogenous storage protein expression, protein body morphology and seed phenotype. To elucidate the molecular mechanisms underlying these changes in transgenic rice seeds, we analyzed the expression profiles of endogenous storage proteins, ER stress-related and programmed cell death (PCD)-related genes in transgenic lines with different levels of Oryza sativa recombinant alpha antitrypsin (OsrAAT) expression. The results indicated that OsrAAT expression induced the ER stress and that the strength of the ER stress was dependent on OsrAAT expression levels. It in turn induced upregulation of the expression of the ER stress response genes and downregulation of the expression of the endogenous storage protein genes in rice endosperm. Further experiments showed that the ER stress response upregulated the expression of PCD-related genes to disturb the rice endosperm development and induced pre-mature PCD. As consequence, it resulted in decrease of grain weight and size. The mechanisms for the detriment seed phenotype in transgenic lines with high accumulation of the recombinant protein were elucidated.
authors.affiliation: State Key Laboratory of Hybrid Rice, Engineering Research Center for Plant Biotechnology and Germplasm Utilization, Ministry of Education, Wuhan, People's Republic of China.
authors.forename: Liping
authors.initials: L
authors.lastname: Zhang
authors.forename: Daiming
authors.initials: D
authors.lastname: Jiang
authors.forename: Jianlei
authors.initials: J
authors.lastname: Pang
authors.forename: Rong
authors.initials: R
authors.lastname: Chen
authors.forename: Xianghong
authors.initials: X
authors.lastname: Wang
authors.forename: Daichang
authors.initials: D
authors.lastname: Yang
mesh_terms: D016923:Cell Death; D059865:Endoplasmic Reticulum Stress; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant; D009929:Organ Size; D012275:Oryza / Q000235:genetics / Q000378:metabolism; D059828:Plant Cells / Q000378:metabolism; D030821:Plants, Genetically Modified / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D055314:Seed Storage Proteins / Q000235:genetics / Q000378:metabolism; D012639:Seeds / Q000254:growth & development*; D015843:Serpins / Q000235:genetics / Q000378:metabolism*; D059467:Transcriptome
chemical_list: D011994:Recombinant Proteins; D055314:Seed Storage Proteins; D015843:Serpins
references.citation: Peptides. 2008 Nov;29(11):1862-70
references.pmid: 18708105
references.citation: Nat Rev Mol Cell Biol. 2012 Jan 18;13(2):89-102
references.pmid: 22251901
references.citation: Plant Mol Biol. 1999 Mar;39(5):915-26
references.pmid: 10344197
references.citation: Nature. 1957 Jun 29;179(4574):1345
references.pmid: 13451615
references.citation: Physiol Rev. 2011 Oct;91(4):1219-43
references.pmid: 22013210
references.citation: Plant J. 2012 Mar;69(6):946-56
references.pmid: 22050533
references.citation: Mol Cell. 2000 Nov;6(5):1099-108
references.pmid: 11106749
references.citation: Proc Natl Acad Sci U S A. 2011 Nov 22;108(47):19078-83
references.pmid: 22042856
references.citation: Planta. 2013 May;237(5):1393-400
references.pmid: 23404671
references.citation: BMC Genomics. 2011 Sep 25;12:462
references.pmid: 21943343
references.citation: Sci Rep. 2012;2:670
references.pmid: 22993695
references.citation: J Exp Bot. 2008;59(3):453-80
references.pmid: 18310084
references.citation: J Histochem Cytochem. 1997 Jan;45(1):89-95
references.pmid: 9010473
references.citation: Apoptosis. 2013 May;18(5):537-46
references.pmid: 23430059
references.citation: Nature. 2002 Jan 3;415(6867):92-6
references.pmid: 11780124
references.citation: Plant J. 2011 Mar;65(5):675-89
references.pmid: 21223397
references.citation: Plant Physiol. 1997 Oct;115(2):737-751
references.pmid: 12223841
references.citation: C R Biol. 2010 Apr;333(4):382-91
references.pmid: 20371113
references.citation: Curr Opin Plant Biol. 1999 Feb;2(1):28-32
references.pmid: 10047564
references.citation: J Plant Physiol. 2013 Jan 15;170(2):202-10
references.pmid: 23043988
references.citation: J Proteome Res. 2009 Feb;8(2):829-37
references.pmid: 18778094
references.citation: Annu Rev Plant Biol. 2013;64:477-99
references.pmid: 23330794
references.citation: Science. 2012 Sep 14;337(6100):1336-40
references.pmid: 22984070
references.citation: J Korean Neurosurg Soc. 2007 Nov;42(5):416-8
references.pmid: 19096582
references.citation: Biochemistry. 2009 Jan 13;48(1):41-9
references.pmid: 19090675
references.citation: Cell. 2001 Dec 28;107(7):881-91
references.pmid: 11779464
references.citation: Trends Plant Sci. 2012 Dec;17(12):720-7
references.pmid: 22796463
references.citation: Mol Microbiol. 2003 Aug;49(3):591-606
references.pmid: 12864846
references.citation: J Biotechnol. 2012 Dec 15;164(2):300-8
references.pmid: 23376844
references.citation: J Cell Sci. 2004 May 15;117(Pt 12):2591-8
references.pmid: 15159454
references.citation: Plant Physiol. 2010 Dec;154(4):1842-54
references.pmid: 20940349
references.citation: Plant Cell Physiol. 2010 Dec;51(12):1964-74
references.pmid: 21037241
references.citation: Mol Biol Cell. 2002 Dec;13(12):4456-69
references.pmid: 12475965
references.citation: Nat Rev Mol Cell Biol. 2007 Jul;8(7):519-29
references.pmid: 17565364
references.citation: Trends Biochem Sci. 2011 Jun;36(6):329-37
references.pmid: 21482118
references.citation: Plant Cell Environ. 2010 Sep;33(9):1453-73
references.pmid: 20082668
references.citation: Planta. 2003 Feb;216(4):597-603
references.pmid: 12569401
references.citation: Genes Dev. 2002 Feb 15;16(4):452-66
references.pmid: 11850408