Cloning and molecular characterization of Triticum aestivum ornithine amino transferase (TaOAT) encoding genes.
Drought tolerance
Floret development
Ornithine aminotransferase
Salt tolerance
Wheat
Journal
BMC plant biology
ISSN: 1471-2229
Titre abrégé: BMC Plant Biol
Pays: England
ID NLM: 100967807
Informations de publication
Date de publication:
29 Apr 2020
29 Apr 2020
Historique:
received:
07
07
2019
accepted:
15
04
2020
entrez:
1
5
2020
pubmed:
1
5
2020
medline:
5
1
2021
Statut:
epublish
Résumé
Ornithine aminotransferase (OAT, EC:2.6.1.13), alternatively known as ornithine delta aminotransferase (δOAT), is a pyridoxal phosphate (PLP)-dependent enzyme involved in the conversion of ornithine into glutamyl-5-semi-aldehyde (GSA) and vice versa. Up till now, there has been no study on OAT in wheat despite the success of its isolation from rice, maize, and sorghum. This study focuses on identification and molecular characterization of OAT in wheat. In total, three homeologous OAT genes in wheat genome were found on chromosome group 5, named as TaOAT-5AL, TaOAT-5BL, and TaOAT-5DL. Sequence alignment between gDNA and its corresponding cDNA obtained a total of ten exons and nine introns. A phylogenetic tree was constructed and results indicated that OATs shared highly conserved domains between monocots and eudicots, which was further illustrated by using WebLogo to generate a sequence logo. Further subcellular localization analysis indicated that they functioned in mitochondria. Protein-protein interactions supported their role in proline biosynthesis through interactions with genes, such as delta 1-pyrroline-5-carboxylate synthetase (P5CS) and pyrroline-5-carboxylate reductase (P5CR), involved in the proline metabolic pathway. Promoter analysis exposed the presence of several stress responsive elements, implying their involvement in stress regulation. Expression profiling illustrated that TaOAT was highly induced in the wheat plants exposed to drought or salt stress condition. Upregulated expression of TaOATs was observed in stamens and at the heading stage. A potential role of TaOAT genes during floret development was also revealed. Furthermore, the transgenic plants overexpressing TaOAT showed enhanced tolerance to drought stress by increasing proline accumulation. In addition, salt tolerance of the transgenic plants was also enhanced. TaOATs genes were involved in proline synthesis and nitrogen remobilization because they interacted with genes related to proline biosynthesis enzymes and arginine catabolism. In addition, TaOAT genes had a role in abiotic stress tolerance and a potential role in floret development. The results of this study may propose future research in the improvement of wheat resistance to abiotic stresses.
Sections du résumé
BACKGROUND
BACKGROUND
Ornithine aminotransferase (OAT, EC:2.6.1.13), alternatively known as ornithine delta aminotransferase (δOAT), is a pyridoxal phosphate (PLP)-dependent enzyme involved in the conversion of ornithine into glutamyl-5-semi-aldehyde (GSA) and vice versa. Up till now, there has been no study on OAT in wheat despite the success of its isolation from rice, maize, and sorghum. This study focuses on identification and molecular characterization of OAT in wheat.
RESULTS
RESULTS
In total, three homeologous OAT genes in wheat genome were found on chromosome group 5, named as TaOAT-5AL, TaOAT-5BL, and TaOAT-5DL. Sequence alignment between gDNA and its corresponding cDNA obtained a total of ten exons and nine introns. A phylogenetic tree was constructed and results indicated that OATs shared highly conserved domains between monocots and eudicots, which was further illustrated by using WebLogo to generate a sequence logo. Further subcellular localization analysis indicated that they functioned in mitochondria. Protein-protein interactions supported their role in proline biosynthesis through interactions with genes, such as delta 1-pyrroline-5-carboxylate synthetase (P5CS) and pyrroline-5-carboxylate reductase (P5CR), involved in the proline metabolic pathway. Promoter analysis exposed the presence of several stress responsive elements, implying their involvement in stress regulation. Expression profiling illustrated that TaOAT was highly induced in the wheat plants exposed to drought or salt stress condition. Upregulated expression of TaOATs was observed in stamens and at the heading stage. A potential role of TaOAT genes during floret development was also revealed. Furthermore, the transgenic plants overexpressing TaOAT showed enhanced tolerance to drought stress by increasing proline accumulation. In addition, salt tolerance of the transgenic plants was also enhanced.
CONCLUSION
CONCLUSIONS
TaOATs genes were involved in proline synthesis and nitrogen remobilization because they interacted with genes related to proline biosynthesis enzymes and arginine catabolism. In addition, TaOAT genes had a role in abiotic stress tolerance and a potential role in floret development. The results of this study may propose future research in the improvement of wheat resistance to abiotic stresses.
Identifiants
pubmed: 32349679
doi: 10.1186/s12870-020-02396-2
pii: 10.1186/s12870-020-02396-2
pmc: PMC7189522
doi:
Substances chimiques
Plant Proteins
0
Polyethylene Glycols
3WJQ0SDW1A
Sodium Chloride
451W47IQ8X
Ornithine-Oxo-Acid Transaminase
EC 2.6.1.13
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
187Subventions
Organisme : National Natural Science Foundation of China
ID : 31771788
Organisme : General Key Program of Science and Technology Department of Ningxia
ID : 2019BBF02020
Références
Plant J. 2018 Nov;96(4):842-854
pubmed: 30144334
Curr Genomics. 2017 Dec;18(6):469-482
pubmed: 29204077
Physiol Plant. 2016 Sep;158(1):45-64
pubmed: 26991441
BMC Plant Biol. 2008 Apr 17;8:40
pubmed: 18419821
Proc Natl Acad Sci U S A. 1980 Dec;77(12):7347-51
pubmed: 7012838
Plant Mol Biol. 2008 May;67(1-2):169-81
pubmed: 18273684
J Biol Chem. 1993 Sep 5;268(25):18673-8
pubmed: 8103048
J Exp Bot. 2015 Jun;66(11):3099-111
pubmed: 25821074
Sci Rep. 2016 Apr 26;6:24978
pubmed: 27113714
J Exp Bot. 2009;60(13):3781-96
pubmed: 19602544
Plant Mol Biol. 2001 Mar;45(4):477-88
pubmed: 11352466
J Plant Physiol. 2012 Jan 1;169(1):41-9
pubmed: 21903295
New Phytol. 2015 Nov;208(3):846-59
pubmed: 26083148
Plant Cell Environ. 2012 Jul;35(7):1329-43
pubmed: 22321246
Plant Biotechnol J. 2017 May;15(5):614-623
pubmed: 27862820
Front Plant Sci. 2018 Aug 07;9:997
pubmed: 30131813
Plant Cell Rep. 2016 Mar;35(3):613-27
pubmed: 26650836
Plant Sci. 2012 Dec;197:59-69
pubmed: 23116672
Int J Mol Sci. 2018 Nov 21;19(11):
pubmed: 30469329
Trends Plant Sci. 2010 Feb;15(2):89-97
pubmed: 20036181
Sci Rep. 2017 Jul 26;7(1):6641
pubmed: 28747704
J Exp Bot. 2011 Jan;62(2):487-95
pubmed: 20952628
Proc Natl Acad Sci U S A. 2010 Jan 5;107(1):490-5
pubmed: 20018663
Nat Genet. 2007 Dec;39(12):1517-21
pubmed: 18026103
Protein Expr Purif. 1998 Apr;12(3):381-9
pubmed: 9535706
Genes Dev. 1998 Apr 15;12(8):1145-54
pubmed: 9553044
Methods Mol Biol. 2015;1223:189-98
pubmed: 25300841
Biochim Biophys Acta. 2012 Feb;1819(2):97-103
pubmed: 22037288
Plant Physiol. 1998 May;117(1):263-71
pubmed: 9576796
Development. 2008 Sep;135(18):3013-9
pubmed: 18701544
Nature. 2012 Nov 29;491(7426):705-10
pubmed: 23192148
Front Plant Sci. 2016 Jan 22;7:4
pubmed: 26834774
Curr Opin Plant Biol. 2003 Oct;6(5):410-7
pubmed: 12972040
BMC Genomics. 2015 Nov 09;16:912
pubmed: 26552372