Difference between revisions of "Os03g0643300"
(Created page with "{{JaponicaGene|
GeneName = Os03g0643300|
Description = Similar to AER123Wp|
Version = NM_001057288.1 GI:115454304 GeneID:4333554|
Length = 7948 bp|
Definition = Oryza sat...") |
(→Structured Information) |
||
| (2 intermediate revisions by 2 users not shown) | |||
| Line 1: | Line 1: | ||
| − | + | An '''ornithine δ-aminotransferase gene''' '''''OsOAT''''' '''confers multi-stress tolerance''' in rice<ref name="ref1"/>. | |
| − | + | ||
| − | + | ==Annotated Information== | |
| − | + | ===Function=== | |
| − | + | ||
| − | + | *''OsOAT'' is a '''direct target''' of the stress-responsive NAC transcription factor '''''SNAC2'''''<ref name="ref2"/>. ''OsOAT'' is responsive to multiple stresses and phytohormone treatments '''mainly through enhancing ROS-scavenging capacity''' and '''Pro pre-accumulation'''. Both '''ABA-dependent''' and '''ABA-independent pathways''' contributed to the '''drought-induced expression''' of ''OsOAT''<ref name="ref1"/>. | |
| − | + | ||
| + | *''OsOAT'' encodes a putative ornithine δ-aminotransferase, was ''upregulated''' in ''SNAC2''-overexpressing plants<ref name="ref2"/>. ''SNAC2'' could '''bind to the promoter fragment''' of ''OsOAT''<ref name="ref1"/>. | ||
| + | |||
| + | '''GO assignment(s):''' [http://amigo.geneontology.org/amigo/term/GO:0008483 GO:0008483],[http://amigo.geneontology.org/amigo/term/GO:0030170 GO:0030170] | ||
| + | |||
| + | ===Mutation=== | ||
| + | Three independent transgenic lines<ref name="ref1"/>: | ||
| + | *OsOAT-OE-7 | ||
| + | *OsOAT-OE-10 | ||
| + | *OsOAT-OE-17 | ||
| + | *The '''δ-OAT activity''' was significantly '''higher''' in the ''OsOAT'' overexpressing lines than in wild-type. | ||
| + | *Under '''normal moisture conditions''', the ''OsOAT'' overexpressing plants '''accumulated significantly more Pro''' than wild-type. | ||
| + | *Under '''drought stress conditions''', the '''free Pro content increased''' in both the transgenic and wild-type plants. However, the '''Pro content''' in the OsOAT-overexpressing lines was slightly '''lower''' than that in the wild-type under drought stress conditions. | ||
| + | *The '''glutathione''' (GSH) '''content''' and '''activity of reactive oxygen species''' (ROS)-scavenging enzymes, such as glutathione peroxidase, were also '''increased''' in OsOAT-overexpressing plants. | ||
| + | |||
| + | ===Expression=== | ||
| + | *Overexpression of the ''OsOAT'' gene in rice resulted in significantly '''enhanced drought and osmotic stress tolerance'''. Overexpression of ''OsOAT'' caused significantly '''increased δ-OAT activity''' and '''Pro accumulation''' under normal growth conditions. In addition, ''OsOAT'' overexpressing plants showed significantly '''increased tolerance to oxidative stress'''<ref name="ref1"/>. | ||
| + | |||
| + | *The '''transcript''' of ''OsOAT'' was '''induced''' in '''leaves''' 3 d after the initiation of drought stress, and the induction increased on day 5 and was maintained on day 7 of the drought stress experiment. The ''OsOAT'' transcript was also '''induced by high-salinity''', '''heat''', and '''submergence'''. transcript of ''OsOAT'' was '''strongly induced by ABA''' and '''IAA''', and it was '''slightly induced by BR''' and '''JA'''<ref name="ref1"/>. | ||
| + | |||
| + | ===Evolution=== | ||
| + | ''OsOAT'' has '''only one splicing mode''' and contains a 1422 bp open reading frame, which is predicted to encode a 473 amino acid protein with a molecular mass of 51.45 kDa. Accordingly, a putative N-terminal transit peptide with a barely conserved sequence for mitochondrial targeting exists in plant and animal δ-OATs including ''OsOAT''. However, such an N-terminal sequence is absent in the δ-OATs from fungal and bacterial species<ref name="ref1"/>. | ||
| + | |||
| + | ===Knowledge Extension=== | ||
| + | *OAT is a mitochondrial enzyme containing pyridoxal-5′-phosphate as a cofactor, which catalyzes the conversion of L-ornithine to L-glutamate γ-semialdehyde using 2-oxoglutarate as a terminal amino group acceptor. It has been described in humans, animals, insects, plants and microorganisms<ref name="ref3"/>. | ||
| + | |||
| + | *Based on the crystal structure of human OAT, both substrate binding and reaction mechanism of the enzyme are well understood<ref name="ref3"/>. | ||
| + | |||
| + | *OAT shows a large structural and mechanistic similarity to other enzymes from the subgroup III of aminotransferases, which transfer an amino group from a carbon atom that does not carry a carboxyl function. In plants, the enzyme has been implicated in proline biosynthesis and accumulation (via pyrroline-5-carboxylate), which represents a way to regulate cellular osmolarity in response to osmotic stress. However, the exact metabolic pathway involving OAT remains a subject of controversy<ref name="ref3"/>. | ||
| + | |||
| + | ==Labs working on this gene== | ||
| + | *National Key Laboratory of Crop Genetic Improvement and National Center of Plant Gene Research (Wuhan), Huazhong Agricultural University, Wuhan 430070, China | ||
| + | |||
| + | ==References== | ||
| + | <references> | ||
| + | * <ref name="ref1"> | ||
| + | You J, Hu H, Xiong L. An ornithine δ-aminotransferase gene OsOAT confers drought and oxidative stress tolerance in rice[J]. Plant Science, 2012, 197: 59-69. | ||
| + | </ref> | ||
| + | * <ref name="ref2"> | ||
| + | Hu H, You J, Fang Y, et al. Characterization of transcription factor gene SNAC2 conferring cold and salt tolerance in rice[J]. Plant molecular biology, 2008, 67(1-2): 169-181. | ||
| + | </ref> | ||
| + | * <ref name="ref3"> | ||
| + | Stránská J, Kopečný D, Tylichová M, et al. Ornithine δ-aminotransferase: an enzyme implicated in salt tolerance in higher plants[J]. Plant signaling & behavior, 2008, 3(11): 929-935. | ||
| + | </ref> | ||
| + | </references> | ||
| + | |||
| + | ==Structured Information== | ||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
[[Category:Genes]] | [[Category:Genes]] | ||
[[Category:Japonica mRNA]] | [[Category:Japonica mRNA]] | ||
Latest revision as of 05:56, 12 June 2015
An ornithine δ-aminotransferase gene OsOAT confers multi-stress tolerance in rice[1].
Contents
Annotated Information
Function
- OsOAT is a direct target of the stress-responsive NAC transcription factor SNAC2[2]. OsOAT is responsive to multiple stresses and phytohormone treatments mainly through enhancing ROS-scavenging capacity and Pro pre-accumulation. Both ABA-dependent and ABA-independent pathways contributed to the drought-induced expression of OsOAT[1].
- OsOAT encodes a putative ornithine δ-aminotransferase, was upregulated' in SNAC2-overexpressing plants[2]. SNAC2 could bind to the promoter fragment of OsOAT[1].
GO assignment(s): GO:0008483,GO:0030170
Mutation
Three independent transgenic lines[1]:
- OsOAT-OE-7
- OsOAT-OE-10
- OsOAT-OE-17
- The δ-OAT activity was significantly higher in the OsOAT overexpressing lines than in wild-type.
- Under normal moisture conditions, the OsOAT overexpressing plants accumulated significantly more Pro than wild-type.
- Under drought stress conditions, the free Pro content increased in both the transgenic and wild-type plants. However, the Pro content in the OsOAT-overexpressing lines was slightly lower than that in the wild-type under drought stress conditions.
- The glutathione (GSH) content and activity of reactive oxygen species (ROS)-scavenging enzymes, such as glutathione peroxidase, were also increased in OsOAT-overexpressing plants.
Expression
- Overexpression of the OsOAT gene in rice resulted in significantly enhanced drought and osmotic stress tolerance. Overexpression of OsOAT caused significantly increased δ-OAT activity and Pro accumulation under normal growth conditions. In addition, OsOAT overexpressing plants showed significantly increased tolerance to oxidative stress[1].
- The transcript of OsOAT was induced in leaves 3 d after the initiation of drought stress, and the induction increased on day 5 and was maintained on day 7 of the drought stress experiment. The OsOAT transcript was also induced by high-salinity, heat, and submergence. transcript of OsOAT was strongly induced by ABA and IAA, and it was slightly induced by BR and JA[1].
Evolution
OsOAT has only one splicing mode and contains a 1422 bp open reading frame, which is predicted to encode a 473 amino acid protein with a molecular mass of 51.45 kDa. Accordingly, a putative N-terminal transit peptide with a barely conserved sequence for mitochondrial targeting exists in plant and animal δ-OATs including OsOAT. However, such an N-terminal sequence is absent in the δ-OATs from fungal and bacterial species[1].
Knowledge Extension
- OAT is a mitochondrial enzyme containing pyridoxal-5′-phosphate as a cofactor, which catalyzes the conversion of L-ornithine to L-glutamate γ-semialdehyde using 2-oxoglutarate as a terminal amino group acceptor. It has been described in humans, animals, insects, plants and microorganisms[3].
- Based on the crystal structure of human OAT, both substrate binding and reaction mechanism of the enzyme are well understood[3].
- OAT shows a large structural and mechanistic similarity to other enzymes from the subgroup III of aminotransferases, which transfer an amino group from a carbon atom that does not carry a carboxyl function. In plants, the enzyme has been implicated in proline biosynthesis and accumulation (via pyrroline-5-carboxylate), which represents a way to regulate cellular osmolarity in response to osmotic stress. However, the exact metabolic pathway involving OAT remains a subject of controversy[3].
Labs working on this gene
- National Key Laboratory of Crop Genetic Improvement and National Center of Plant Gene Research (Wuhan), Huazhong Agricultural University, Wuhan 430070, China
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 You J, Hu H, Xiong L. An ornithine δ-aminotransferase gene OsOAT confers drought and oxidative stress tolerance in rice[J]. Plant Science, 2012, 197: 59-69.
- ↑ 2.0 2.1 Hu H, You J, Fang Y, et al. Characterization of transcription factor gene SNAC2 conferring cold and salt tolerance in rice[J]. Plant molecular biology, 2008, 67(1-2): 169-181.
- ↑ 3.0 3.1 3.2 Stránská J, Kopečný D, Tylichová M, et al. Ornithine δ-aminotransferase: an enzyme implicated in salt tolerance in higher plants[J]. Plant signaling & behavior, 2008, 3(11): 929-935.
