Difference between revisions of "Os02g0606700"
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RSS1 ensures cell division activity under stress conditions[1]. In agreement with the proposed function of RSS1, genes involved in the cell cycle and DNA replication were preferentially downregulated in rss1 under high-salt conditions. Conspicuously, more than 30% of the genes that were expressed specifically in the shoot apex were coordinately downregulated in rss1 under high-salt conditions , supporting the proposed function of RSS1 in maintaining proliferative tissue activity[1]. RSS1 functions preferentially in dividing cells, and its stability is regulated by cell cycle phase-dependent protein degradation through the aphase-promoting complex/cyclosome (APC/C)26S proteasome pathway. Moreover, RSS1 interacts with a type 1 protein phosphatase (PP1), which regulates many cellular processes, including the cell division cycle[2-6]. | RSS1 ensures cell division activity under stress conditions[1]. In agreement with the proposed function of RSS1, genes involved in the cell cycle and DNA replication were preferentially downregulated in rss1 under high-salt conditions. Conspicuously, more than 30% of the genes that were expressed specifically in the shoot apex were coordinately downregulated in rss1 under high-salt conditions , supporting the proposed function of RSS1 in maintaining proliferative tissue activity[1]. RSS1 functions preferentially in dividing cells, and its stability is regulated by cell cycle phase-dependent protein degradation through the aphase-promoting complex/cyclosome (APC/C)26S proteasome pathway. Moreover, RSS1 interacts with a type 1 protein phosphatase (PP1), which regulates many cellular processes, including the cell division cycle[2-6]. | ||
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Revision as of 04:18, 17 May 2014
RSS1 ensures cell division activity under stress conditions.
Contents
Annotated Information
Function
RSS1 ensures cell division activity under stress conditions[1]. In agreement with the proposed function of RSS1, genes involved in the cell cycle and DNA replication were preferentially downregulated in rss1 under high-salt conditions. Conspicuously, more than 30% of the genes that were expressed specifically in the shoot apex were coordinately downregulated in rss1 under high-salt conditions , supporting the proposed function of RSS1 in maintaining proliferative tissue activity[1]. RSS1 functions preferentially in dividing cells, and its stability is regulated by cell cycle phase-dependent protein degradation through the aphase-promoting complex/cyclosome (APC/C)26S proteasome pathway. Moreover, RSS1 interacts with a type 1 protein phosphatase (PP1), which regulates many cellular processes, including the cell division cycle[2-6].
Expression
RSS1 mRNA is expressed abundantly in proliferating tissue, such as the basal region of the shoot, which contains apical and lateral shoot meristems and leaf primordia, and to a lesser extent, in the upper region of the shoot. RSS1 expression was upregulated by low temperatures, but not by high-salt conditions Supplementary[1].
Labs working on this gene
1
Bioscience and Biotechnology Center, Nagoya University, Chikusa, Nagoya 464-8601, Japan
2
National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan
3
RIKEN Plant Science Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
4
Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan. Correspondence and requests for material should be addressed to H.H. (hirohiko@nias.affrc.go.jp) or to S.T. (takeda@agr.nagoya-u.ac.jp).
References
1、Ogawa D, Abe K, Miyao A, et al. RSS1 regulates the cell cycle and maintains meristematic activity under stress conditions in rice[J]. Nature communications, 2011, 2: 278.
2. Goldberg, J. et al. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 376, 745–753 (1995).
3. Berndt, N., Dohadwala, M. & Liu, C. W. Constitutively active protein phosphatase 1alpha causes Rb-dependent G1 arrest in human cancer cells. Curr. Biol. 7, 375–386 (1997).
4. Cohen, P. T. Protein phosphatase 1—targeted in many directions. J. Cell Sci.115, 241–256 (2002).
5. Ceulemans, H. & Bollen, M. Functional diversity of protein phosphatase-1,a cellular economizer and reset button. Physiol. Rev. 84, 1–39 (2004).
6. Hirschi, A. et al. An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein. Nat. Struct. Mol. Biol. 17, 1051–1057 (2010).
Structured Information
| Gene Name |
Os02g0606700 |
|---|---|
| Description |
Conserved hypothetical protein |
| Version |
NM_001053915.1 GI:115447200 GeneID:4329928 |
| Length |
3394 bp |
| Definition |
Oryza sativa Japonica Group Os02g0606700, 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 2:24627261..24630654 |
| Sequence Coding Region |
24628264..24628321,24628406..24628774,24628878..24628963,24629955..24630042,24630164..24630294 |
| Expression | |
| Genome Context |
<gbrowseImage1> name=NC_008395:24627261..24630654 source=RiceChromosome02 preset=GeneLocation </gbrowseImage1> |
| Gene Structure |
<gbrowseImage2> name=NC_008395:24627261..24630654 source=RiceChromosome02 preset=GeneLocation </gbrowseImage2> |
| Coding Sequence |
<cdnaseq>atggctgccccaactgcaacagctgtttttcttgatgagaacctgcatatccatagggggcctgctggcaagagggctgatggattgaaggccaagccactgaagccattagcagcaaagcaagggcttcaagagaagaaggccctgagggatgtatccaacattggcaagcccccggtgtctacgcggaagcccctgcaggacgtgtccaacaccgccaagccccgagggcgcaacatttctgatggcactaccttgaagaagactgctcttcgcagccatgaggccaccaagaacccagtgaagaagactgtaatcttttctgatgagaccgcaaaatgtcatgaatgggctaaggatggggtggagggcacccacttcactgggaatgattctcagaagttggaaaaggacagtcaagacaaacgtgtcaagaagaaggtggagaaaataatgtcagcattgcacgactggccagacgcggtatttgatcatgtgctttttccatctgaggtggtagcagcgttttttgaagaagtaaaagagatggagctggaacctgagattcttccagagaacaataggcgtcgctcaagttcaggtgataaaatgaagctggctgaagatcctttcacggaagacgagcttgactactacccatttcttgagaacaatcccgttgagtttcagctgagagatgagctaccactcctggagcctggaatgaactga</cdnaseq> |
| Protein Sequence |
<aaseq>MAAPTATAVFLDENLHIHRGPAGKRADGLKAKPLKPLAAKQGLQ EKKALRDVSNIGKPPVSTRKPLQDVSNTAKPRGRNISDGTTLKKTALRSHEATKNPVK KTVIFSDETAKCHEWAKDGVEGTHFTGNDSQKLEKDSQDKRVKKKVEKIMSALHDWPD AVFDHVLFPSEVVAAFFEEVKEMELEPEILPENNRRRSSSGDKMKLAEDPFTEDELDY YPFLENNPVEFQLRDELPLLEPGMN</aaseq> |
| Gene Sequence |
<dnaseqindica>1004..1061#1146..1514#1618..1703#2695..2782#2904..3034#aaagcaaaaaaatttcccctttcctctccacgccaagaaacgcaaaacccccacgccgaccaaggcgagaagcgccgccgccgaatcgaaccgcgatcgcgcccttctcccgccgcccccgcgcgctcttctcctcctcgtcctcgacgccgctgtgccggagtttaggcggagatcgatccggagcggggtttctcttctacctggtaggtaagcactggggctttctcttggattggtcacgcgttgtcttgaatttttttttcccgtcatcgaggaaaattttgccctatcttgctcgtttcttggttgttggtgaccgaatccaaaccctaggttatccgcaacattccggtccaattcgtgcaaactggcatgttattggggatttgtttgctcctgctaatttcatgaaatacgtatggctcgggtcccttggaagattttaggtgcgtcgtctaatctgttagtttggaacccggagcaaaatatttctgagctgtcgctgcaaatctgttggagaaacggctgtgtcccttgaagactctaggtgcgccgtctaatctgttacttcctccgtttcacaatataagtcattctagtatttcccacattcatattgatactaatgaatctagatagatatagtctagatccattggcatcaatatgaatgtgggaaatggtggaatgacttacattatgaaacggagggagtagtttagaacgcaaagcaaaatatttctgatattttgctgaaaatctgttggagaaatggggactcatgcagaatgtatgtgaaatcctggtttccttcagcaaccatatgttgttatgctacaagttgaactaatatttttctgaccatgtgcaaaatttgtagaacaaaatgtgtaatatatactgcttattgtttttctctagcaattttgtcttttccccctttgctcagtacctagaatttttcaggcaaggttgaggaagaaaagcttgctgatttgtgatggctgccccaactgcaacagctgtttttcttgatgagaacctgcatatccataggggtaaggctgcttttgatctgactaattcatcacaaggaggatttcctgtggtaaatgactgacatgtttggtccatgtgtgcagggcctgctggcaagagggctgatggattgaaggccaagccactgaagccattagcagcaaagcaagggcttcaagagaagaaggccctgagggatgtatccaacattggcaagcccccggtgtctacgcggaagcccctgcaggacgtgtccaacaccgccaagccccgagggcgcaacatttctgatggcactaccttgaagaagactgctcttcgcagccatgaggccaccaagaacccagtgaagaagactgtaatcttttctgatgagaccgcaaaatgtcatgaatgggctaaggatggggtggagggcacccacttcactgggaatgattctcagaagttggaaaaggacagtcaagacaaacgtaagagttcacttcctgcagttcaatatgccatagaacccttttgctttcagtaggctcagataatgagataacttgttttgttattgttcattctacacaggtgtcaagaagaaggtggagaaaataatgtcagcattgcacgactggccagacgcggtatttgatcatgtgctttttccatctgaggtatgtatttcaaagagcacagtgttcagacttttccagattgcttttacttttgaaatatttctgtggatttgaatttcaaggtcgaagaagaaagcttttgattttttctatgtacaaatacactacctaacttggctaactagcttggctgataatttattgaatctagaagagcctcaagtattgcttgatctctacataccttttgcgtgaacagtagctgatgcctggtggtatcatttgacacaagaagataactaatgggtacatagtaaattaatgactaggccagtattttatgttttctgtcgcaaaacaatagtggtggtatcatttgacaagcttattcttgttattttatctgtcatttgacaagcttaattgggctatttccctgtaatattctcttatattaagagaaaaaaaagtctattctgaattatactattccctgaatgaaactgttatctggatattgatggattcccttttgctaccagtagtgcttgtctttatttatttccaagctggctgacttatttcattgtggttcctctatttatatttatgcttaataatagtattcactggcatcagaagaagccagaaaggggacttctatgattcggtatgacattggtttcgctaaaagttaactcatggatgagaaaaccttacatgtattttaatagctaacaacagagaacatccatgataccgtcatgggtcagtaacagttaaaatgtttgatggttattaattgtggtatgttcttctgtctgtacatggttctgtttgatgaactgctcggtcattcattcatgctctgaagtctgaagcaacatgttattctagggataaattatgtcttgctctatgtcgataacatttcttgctttcttgtatcttttcttcttgatctccaatatgttatgtgattatctcaagcaacgcagatgcaatgctaattgtttttcaatgtatataggtggtagcagcgttttttgaagaagtaaaagagatggagctggaacctgagattcttccagagaacaataggcgtcgctcaagttcaggtctctttcttcttccttgcacacattcatgccgttctctcatctctgctttccagtgcttccatcaacaacatcgtctcgatttcttccttataatctgtatggatgtttgcccctccaggtgataaaatgaagctggctgaagatcctttcacggaagacgagcttgactactacccatttcttgagaacaatcccgttgagtttcagctgagagatgagctaccactcctggagcctggaatgaactgaagaatgctaatctgccccacttgaaaagacctcagaacagtgctattatcatcattatcctctttgcaaactctacttgctcaggagcagtttatttgtagtagtagtagtagtaactagtatcctagatgttctgctgtatgtggttggtgtgataatcattcacactttaggaagaacccaagtagcggaagcaactttagcttcctttatgttctgtgtcttggctgaaatacccatcattaagccattgtgtaaatggtagtagtagtaaactgtagtgtaaggattctgcagaagtacatgcgtgtgccacttcctctattacgaatgcgtgcacatgtgtttgatttcctgttt</dnaseqindica> |
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