Difference between revisions of "Os06g0700700"
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===Mutation=== | ===Mutation=== | ||
| − | ''OsHMA2'' is composed of nine exons and eight introns. Secondary structure prediction of membrane proteins, an online bioinformatics tool, predicted that the OsHMA2 protein in the wild type has six transmembrane segments and a histidine-rich C-terminal domain. To investigate the function of ''OsHMA2'', three the retrotransposon ''Tos17'' insertion mutants were obtained. The ''Tos17'' insertion into intron 5 was designated ''oshma2-1''.In other two lines the insertions were in exon 9 at different positions. Only two transmembrane segments occur in oshma2-1 according to SOSUI predition. In ''oshma2-2'', most of the C-terminal region after the last transmembrane segment is absent, and in ''oshma2-3'', only part of the histidine-rich C-terminal region is absent. <ref name="ref2"/ > | + | ''OsHMA2'' is composed of nine exons and eight introns. Secondary structure prediction of membrane proteins, an online bioinformatics tool, predicted that the OsHMA2 protein in the wild type has six transmembrane segments and a histidine-rich C-terminal domain. To investigate the function of ''OsHMA2'', three the retrotransposon ''Tos17'' insertion mutants were obtained. The ''Tos17'' insertion into intron 5 was designated ''oshma2-1''.In other two lines the insertions were in exon 9 at different positions. Only two transmembrane segments occur in oshma2-1 according to SOSUI predition. In ''oshma2-2'', most of the C-terminal region after the last transmembrane segment is absent, and in ''oshma2-3'', only part of the histidine-rich C-terminal region is absent. <ref name="ref2"/> |
| − | When grow wild type and three ''oshma2'' mutants with 4.5nM Cd, oshma2 mutants had a significantly lower translocation ratio of Cd and Zn than the wild type. The concentrations of Cd and Zn in shoots of the ''oshma2'' mutants were very low. And the concentration of Cd in the roots of oshma2 mutants were not significantly different from those of wild type, while the concentration of Zn in roots of oshma2 mutants higher than the wild type.<ref name="ref2"/ > | + | When grow wild type and three ''oshma2'' mutants with 4.5nM Cd, oshma2 mutants had a significantly lower translocation ratio of Cd and Zn than the wild type. The concentrations of Cd and Zn in shoots of the ''oshma2'' mutants were very low. And the concentration of Cd in the roots of oshma2 mutants were not significantly different from those of wild type, while the concentration of Zn in roots of oshma2 mutants higher than the wild type.<ref name="ref2"/> |
===Evolution=== | ===Evolution=== | ||
Revision as of 11:22, 1 June 2014
OsHMA2 is a transporter of Zn and Cd in rice and involved in the root-to-shoot translocation of Zn and Cd.
Contents
Annotated Information
Function
The P1B-type heavy metal ATPases(HMA) are transporters which play an important role in the translocation or detoxification of Zn or Cd in plants. These transporters are divided into two subgroups based on their metal-substrate specificity: a copper (Cu)/silver (Ag) group and a zinc (Zn)/cobalt (Co)/cadmium (Cd)/lead (Pb) group. Rice(Oryza sativa L.) has nine HAM genes. OsHMA2 belongs to the Zn/Co/Cd/Pb subgroup. OsHMA2 is a gene which is localized in the plasma membrane and trasport Zn and Cd out of the cell. [2] OsHMA2 plays an important role in the root-to-shoot translocation of Zn and Cd, and participate in Zn and Cd transport to developing seeds in rice. In rice, OsHMA2 is the only gene which is responsible for the translocation of Zn, unlike Arabidopsis, in which two genes have redundant fuctions. OsHMA2 is also the transporter of Cd in rice and to date, the OsHMA2 is the only one gene which translocate both Zn and Cd in rice. [3] OsHMA2 also plays a role in Zn transport during flowering and seed maturing. [2]
Expression
Total RNA was extracted from rice using the RNeasy Plant Mini Kit. The RNA was reverse transcribed using an oligo dT primer and the ReverTra Ace reverse transcriptase. Amplification reactions were carried out with the HMA2-F1 primer (5′-GCAGATCAAGTCACCCCATGG-3′) and the HMA2-R1 primer (5′-GCCATCACCAAC CATCAGCGT-3′). As an internal standard, the a-tubulin gene was used as described previously. Transcript abundance was normalized by a-tubulin expression level, and the results represent average number of copies of OsHMA2 transcripts in 1 mg of total RNA in three reactions.[1]
The expression of OsHMA2 was observed mainly in the roots. Using LM, OsHMA2 transcripts were detected mainly in vascular bundles. Expression of OsHMA2 in the roots was unchanged in the presence of Cd, whereas expression in the shoots increased in the presence of 1 mm Cd. Under Zn deficiency, the expression of OsHMA2 decreased in the roots, whereas it remained unchanged in shoots. In contrast, the expression of OsHMA2 increased in roots under Fe deficiency, whereas it decreased in shoots. Expression of OsHMA2 was unchanged in both roots and shoots under Mn deficiency.[1]
Mutation
OsHMA2 is composed of nine exons and eight introns. Secondary structure prediction of membrane proteins, an online bioinformatics tool, predicted that the OsHMA2 protein in the wild type has six transmembrane segments and a histidine-rich C-terminal domain. To investigate the function of OsHMA2, three the retrotransposon Tos17 insertion mutants were obtained. The Tos17 insertion into intron 5 was designated oshma2-1.In other two lines the insertions were in exon 9 at different positions. Only two transmembrane segments occur in oshma2-1 according to SOSUI predition. In oshma2-2, most of the C-terminal region after the last transmembrane segment is absent, and in oshma2-3, only part of the histidine-rich C-terminal region is absent. [3]
When grow wild type and three oshma2 mutants with 4.5nM Cd, oshma2 mutants had a significantly lower translocation ratio of Cd and Zn than the wild type. The concentrations of Cd and Zn in shoots of the oshma2 mutants were very low. And the concentration of Cd in the roots of oshma2 mutants were not significantly different from those of wild type, while the concentration of Zn in roots of oshma2 mutants higher than the wild type.[3]
Evolution
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Labs working on this gene
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References
Structured Information
| Gene Name |
Os06g0700700 |
|---|---|
| Description |
Similar to P1B-type heavy metal transporting ATPase |
| Version |
NM_001065015.1 GI:115469761 GeneID:4341965 |
| Length |
2957 bp |
| Definition |
Oryza sativa Japonica Group Os06g0700700, complete gene. |
| Source |
Oryza sativa Japonica Group ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
| Chromosome | |
| Location |
Chromosome 6:30354951..30357907 |
| Sequence Coding Region |
30355990..30356270,30357298..30357487 |
| Expression | |
| Genome Context |
<gbrowseImage1> name=NC_008399:30354951..30357907 source=RiceChromosome06 preset=GeneLocation </gbrowseImage1> |
| Gene Structure |
<gbrowseImage2> name=NC_008399:30354951..30357907 source=RiceChromosome06 preset=GeneLocation </gbrowseImage2> |
| Coding Sequence |
<cdnaseq>atggcggcggagggagggaggtgtcagaagagctacttcgacgtgctggggatttgctgcccgtcggaggttcccctcgtcgagaagcttctgcagccgctggagggcgtccagaaggtcaccgtgatcgttccctccaggacggtcatcgtcgtccacgacgtcgacgccatctcccaatcccaaatcgtcaaggcgctgaatcaggcaaggttggaggcgtcggttcgggcttatgggaacggcagtgagaagatcaccaacaaatggccgagcccgtatgttctcctctgcggacttcttctggtcgtgtcgctgttcgagcatttctggcacccgctcaagtggttcgcgctggtggctgcggccgccggcttgccgccgatcgtgctgaggagcattgcggccatccggagactcaccctggatgtcaacatactcatgctgattgctggtaagaacagcctataa</cdnaseq> |
| Protein Sequence |
<aaseq>MAAEGGRCQKSYFDVLGICCPSEVPLVEKLLQPLEGVQKVTVIV PSRTVIVVHDVDAISQSQIVKALNQARLEASVRAYGNGSEKITNKWPSPYVLLCGLLL VVSLFEHFWHPLKWFALVAAAAGLPPIVLRSIAAIRRLTLDVNILMLIAGKNSL</aaseq> |
| Gene Sequence |
<dnaseqindica>1638..1918#421..610#ctatccccgattcgcacagccaatctcttcttgcttcctcctcctcctcctccagccgccgccgccgacgacgattcttggtagagagattcttgcgttgttttacctgcgtcttgttcttcttgggagttgggtggatcgattgatcgaggttttggaggttggaagaagtgtgtgttgtggtggggggtaagtgagatggagaactgaattcactgaactcattttctttccttttttttttggtctgacaagaagtaaaaattcctgaacctgaaaccaaccaaaggacaggttggtcgacacgccaagattgcttttgctgctgtgtccttctcactcttgttcttgttcttgcttcttcaggtttgtagagagagagagggcaaaggcacgcaaagagggagagagtgaggagagatggcggcggagggagggaggtgtcagaagagctacttcgacgtgctggggatttgctgcccgtcggaggttcccctcgtcgagaagcttctgcagccgctggagggcgtccagaaggtcaccgtgatcgttccctccaggacggtcatcgtcgtccacgacgtcgacgccatctcccaatcccaaatcggtgagagccccccttttttcttttttgctttccgagtggattgattcatctccctttcgtgattaagatcgatctctccttccatcttgacttgtcacttatcattgtcctgtgatcaatgaatgataccaatcatgcaaccggtgactgagccatcttgtgggatttgtggagtttttgggtgggtcaagaagtcacacgagactagaccagaccagagtctcagtaatttgaagaaaacgatcttttttattttctttgtcatggctgcttgtttgttcattggattttcgatgattttatttctgttcttgctagtttaatcagaatcttactttaattatcgcaagaaaaattggatcttaacatatatatagcgtgttgagcgatggaaagcatcacgcaaagttgcttgcgtttctcattctgttcttgctgttcatgagttgttccagtatctgtattttttttttgtttgtttgtttgtttgttcacaataaatttcatttctaatcgttgcttgattcaataactagccagccaagcaaaggtggtgtcatgtgttcgtttgttttcatggctcgaggctggggaccacttaccatgtcagaaaataagtgcaaaatttcatactccaactctactaaaatgggatgtttgctagcgacaagtgaaccgtcttggcagtggtcgctattgttcatgacgcagggagcaattactgatacgattggacatatctcttgactcgttaattctgacctcagcacccccgaaatcctgctaattttgcagtttctgtcacgagaattaaggaacttgattactgtacaatactgtcacactcaatgaaaccgccagtttttcatctttggttcttgaaacagtcattacataattttagataaatgttactgtccttgaggaggtataccaattatgacagatggacagtaaaatcaatcacgattttagcatgacaaaactcttgaaagcttgatttgattttgatatttgctgttttcagtcaaggcgctgaatcaggcaaggttggaggcgtcggttcgggcttatgggaacggcagtgagaagatcaccaacaaatggccgagcccgtatgttctcctctgcggacttcttctggtcgtgtcgctgttcgagcatttctggcacccgctcaagtggttcgcgctggtggctgcggccgccggcttgccgccgatcgtgctgaggagcattgcggccatccggagactcaccctggatgtcaacatactcatgctgattgctggtaagaacagcctataattcacctgtgacattaatgatgtttcctgttattggtaccttgaaaaaaaaagaagctcccttttgttggaggatggccctgaccatcacctccgacgatcgaagaccctttgatctttaggagataactgaattataaaattttaaataggcttccttcatctggtggcctaatgcatgcattttggcttgtaccaaaacctactttctctctttaatgaaatgaaaagcagaggtcccaccatactttttgaaaagaaatgaacgtttaaatagtatcgaatggtagcaaacacatctgccattaaggatatcctccaattgaatagtctcatttgaaataagaaaacaaattattgacacagcttagtagtagagcattgagttttaacgttgatgccatgggtttgaagcttttttttctgtattaaaagggcaacagtatacttgttcctttttttaccatagtattctcttgtgtgtagaagacacaaatacaacaccactttgggtaaatattcaactacggattgaagttgtgggtattattgatacctgttctaccagtgtgacaatgggttgtgaaaaaaaaagagacaaaagcaagtttcttcacgaggaccaatatggtgggtgattagtgggagagcagaagcagaaatccatctctcaaaagtttatgtctcacttgcataaacttttgctttcttttcttttctagagggtccctcactttccatcacatcaaaaggatatgttgctgtgatgctaatatacgtgctagatgaacaattctgcttcttttcctccatgtggcgatgtcacctcagatagggcatcagattccttttagaacaagcaacatatttcttatcaagaagctacacatatttcgaataattctttctagactaatatcgtggcattgagatagctctattgtgatatgcatatgggaatatgggatacatgaaagaatcatcaaaagaaacaagaaataccttgtttcaaaaagaaaaaaagatttggaagatttggt</dnaseqindica> |
| External Link(s) |
- ↑ 1.0 1.1 1.2 1.3 1.4 Ryuichi Takahashi, Yasuhiro Ishimaru, Hugo Shimo, Yuko Ogo, Takeshi Ssnoura, Naoko K. Nishizawa and Hiromi Nakaishi.(2012) The OsHMA2 transporter is involved in root-to-shoot translocation of Zn and Cd in rice. Plant, Cell and Environment 35:1948–1957.
- ↑ 2.0 2.1 2.2 Ryuichi Takahashi, Khurram Bashir, Yasuhiro Ishimaru, Naoko K. Nishizawa and Hiromi Nakanishi.(2012) The role of heavy-metal ATPases, HMAs, in zinc and cadmium transport in rice. Plant Signaling & Behavior 7:12, 1605–1607.
- ↑ 3.0 3.1 3.2 3.3 Namiko Satoh-Nagasawa, Mikako Mori, Nobushige Nakazawa, Tomohiko Kawamot3, Yasuo Nagato, Kenji Sakurai, Hidekazu Takahashi, Akio Watanabe and Hiromori Akagi.(2012) Mutations in Rice (Oryza sativa) Heavy Metal ATPase2 (OsHMA2) Restrict the Translocation of Zinc and Cadmium. Plant Cell Physiol 53(1): 213–224.
