Isolation and characterization of S-Adenosylmethionine synthase gene from cucumber and responsive to abiotic stress.
Antioxidants
/ metabolism
Arabidopsis
/ metabolism
Cucumis sativus
/ enzymology
Droughts
Gene Expression Profiling
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Plant
Hydrogen Peroxide
/ chemistry
Methionine Adenosyltransferase
/ genetics
Phylogeny
Plant Proteins
/ genetics
Plants, Genetically Modified
Polyamines
/ chemistry
Salt Tolerance
Salts
Stress, Mechanical
Stress, Physiological
/ genetics
Nicotiana
/ metabolism
Cucumis sativus
Function
Gene expression
S-adenosylmethionine synthetase
Salt stress
Journal
Plant physiology and biochemistry : PPB
ISSN: 1873-2690
Titre abrégé: Plant Physiol Biochem
Pays: France
ID NLM: 9882449
Informations de publication
Date de publication:
Aug 2019
Aug 2019
Historique:
received:
22
04
2019
revised:
12
05
2019
accepted:
06
06
2019
pubmed:
27
6
2019
medline:
6
8
2019
entrez:
26
6
2019
Statut:
ppublish
Résumé
S-adenosylmethionine synthetase (SAMS) catalyzes methionine and ATP to generate S-adenosyl-L-methionine (SAM). In plants, accumulating SAMS genes have been characterized and the majority of them are reported to participate in development and stress response. In this study, two putative SAMS genes (CsSAMS1 and CsSAMS2) were identified in cucumber (Cucumis Sativus L.). They displayed 95% similarity and had a high identity with their homologous of Arabidopsis thaliana and Nicotiana tabacum. The qRT-PCR test showed that CsSAMS1 was predominantly expressed in stem, male flower, and young fruit, whereas CsSAMS2 was preferentially accumulated in stem and female flower. And they displayed differential expression profiles under stimuli, including NaCl, ABA, SA, MeJA, drought and low temperature. To elucidate the function of cucumber SAMS, the full-length CDS of CsSAMS1 was cloned, and prokaryotic expression system and transgenic materials were constructed. Expressing CsSAMS1 in Escherichia coli BL21 (DE3) improved the growth of the engineered strain under salt stress. Overexpression of CsSAMS1 significantly increased MDA content, H
Identifiants
pubmed: 31238253
pii: S0981-9428(19)30241-4
doi: 10.1016/j.plaphy.2019.06.006
pii:
doi:
Substances chimiques
Antioxidants
0
Plant Proteins
0
Polyamines
0
Salts
0
Hydrogen Peroxide
BBX060AN9V
Methionine Adenosyltransferase
EC 2.5.1.6
Types de publication
Journal Article
Langues
eng
Pagination
431-445Informations de copyright
Copyright © 2019 Elsevier Masson SAS. All rights reserved.