Difference between revisions of "Os02g0203500"
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| − | RLS1 encodes a previouslyuncharacterized NB (nucleotide-binding site)-containing protein with an ARM (armadillo) domain at the carboxyl terminus .<ref name="ref1"> Bin-Bin Jiao;Jian-Jun Wang;Xu-Dong Zhu;Long-Jun Zeng;Qun Li;Zu-Hua He . A Novel Protein RLS1 with NB–ARM Domains Is Involved in Chloroplast Degradation during Leaf Senescence in Rice Molecular Plant, 2012, 5(1): 205-217</ref> | + | The RLS1 locus was roughly mapped on chromosome 2. And it encodes a previouslyuncharacterized NB (nucleotide-binding site)-containing protein with an ARM (armadillo) domain at the carboxyl terminus .Consistent with its involvement in leaf senescence, RLS1 was up-regulated during dark-induced leaf senescence |
| + | and down-regulated by cytokinin. Intriguingly, constitutive expression of RLS1 also slightly accelerated leaf senescence with decreased chlorophyll content in transgenic rice plants.<ref name="ref1"> Bin-Bin Jiao;Jian-Jun Wang;Xu-Dong Zhu;Long-Jun Zeng;Qun Li;Zu-Hua He . A Novel Protein RLS1 with NB–ARM Domains Is Involved in Chloroplast Degradation during Leaf Senescence in Rice Molecular Plant, 2012, 5(1): 205-217</ref> | ||
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===Function=== | ===Function=== | ||
| − | 1.Map-based cloning of the RLS1 gene revealed that it encodes a previously uncharacterized NB (nucleotide-binding site)-containing protein with an ARM (armadillo) domain at the carboxyl terminus.<ref name="ref1" /> | + | 1.Map-based cloning of the RLS1 gene revealed that it encodes a previously uncharacterized NB (nucleotide-binding site)-containing protein with an ARM (armadillo) domain at the carboxyl terminus.The rls1 mutant displayed accelerated leaf senescence in both natural and dark-induced senescence, in comparison with the |
| + | wild-type. We found that PCD involved in chloroplast degradation was misregulated in the leaf cells of rls1. Map-based cloning revealed that RLS1 encodes a novel NB containing protein with an ARM domain that presents only in sorghum, grape, and black cottonwood genomes.<ref name="ref1" /> | ||
2.Consistent with its involvement in leaf senescence, RLS1 was up-regulated during dark-induced leaf senescence and down-regulated by cytokinin.<ref name="ref1" /> | 2.Consistent with its involvement in leaf senescence, RLS1 was up-regulated during dark-induced leaf senescence and down-regulated by cytokinin.<ref name="ref1" /> | ||
| − | 3.Intriguingly, constitutive expression of RLS1 also slightly accelerated leaf senescence with decreased chlorophyll content in transgenic rice plants.<ref name="ref1" /> | + | 3.Intriguingly, constitutive expression of RLS1 also slightly accelerated leaf senescence with decreased chlorophyll content in transgenic rice plants.The rls1 mutant plants showed accelerated leaf senescence under both natural and dark-induced conditions(Figure 1A, 1C, and 1D） . Therefore, the accelerated senescence of the rls1 mutant appears not to be directly induced by the formation of spontaneous lesions.The rapid loss of chlorophyll was the main cause of accelerated leaf senescence in rls1.<ref name="ref1" />[[File:RLS1.00.png|none|300px]] [[File:RLS1.0.png|none|300px]] (figure1)<ref name="ref1" /> |
| − | 4. | + | 4. The RLS1 gene might be involved in PCD that affects specific cellular processes.previously uncharacterized NB–ARM protein involved in PCD during plant growth and development, providing a unique tool for dissecting possible autophagymediated PCD during senescence in plants.<ref name="ref1" /> |
| − | 5. RLS1 Is necessary for proper Chloroplast degradation. | + | 5. RLS1 Is necessary for proper Chloroplast degradation.The mutation in the RLS1 accelerates the degradation of chloroplasts probably through an autophagy-mediated partial degradation process<ref name="ref1" /> |
===Expression=== | ===Expression=== | ||
| − | 1.There is only one copy of the RLS1 gene in the rice genome. The RLS1 homolog genes with unknown function were only found in sorghum, grape, and black cottonwood by a BLAST search. The putative NB domain of RLS1 contains the conserved motifs found in a large number of proteins binding ATP or GTP, and shows a significant similarity to that of homologous proteins from sorghum, grape, and black cottonwood. | + | 1.There is only one copy of the RLS1 gene in the rice genome. The RLS1 homolog genes with unknown function were only found in sorghum, grape, and black cottonwood by a BLAST search. The putative NB domain of RLS1 contains the conserved motifs found in a large number of proteins binding ATP or GTP, and shows a significant similarity to that of homologous proteins from sorghum, grape, and black cottonwood. Genetic studies have provided evidence that NB-containing R proteins in plant, such as RPS4, RPM1, can activate cell death during HR execution (Hofius et al., 2009<ref name="ref2" />).<ref name="ref1" /> |
| − | 2. RLS1 expression Is affected by dark-induced senescence and Cytokinin treatment. | + | 2. RLS1 expression Is affected by dark-induced senescence and Cytokinin treatment. The expression of RLS1 was significantly induced in the seedlings transferred into darkness and reached the maximum level 12 h after treatment (Figure2). Accumulation of the RLS1 transcript was markedly reduced in the seedlings treated with 20 lM trans-zeatin (tZ) for 24 h (Figure1). These results suggested that RLS1 is involved in leaf senescence.<ref name="ref1" /> [[File:RLS1.1.png|none|300px]] (figure2)<ref name="ref1" /> |
| − | 3. The expression profile of RLS1 was investigated in various rice tissues at the adult stage with the quantitative real-time PCR approach. The results showed that RLS1 transcripts accumulated constitutively during leaf development, from young to senescent leaves (Figure | + | 3. The expression profile of RLS1 was investigated in various rice tissues at the adult stage with the quantitative real-time PCR approach. The results showed that RLS1 transcripts accumulated constitutively during leaf development, from young to senescent leaves (Figure 2). In addition, RLS1 was constitutively but |
weakly expressed in the root of seedling, panicle, and spikelet. The highest level of the RLS1 transcript was detected in mature leaves, consistent with the phenotype of rls1.<ref name="ref1" /> | weakly expressed in the root of seedling, panicle, and spikelet. The highest level of the RLS1 transcript was detected in mature leaves, consistent with the phenotype of rls1.<ref name="ref1" /> | ||
| − | 4. Overexpression of RLS1 displays a weak Phenotype of accelerated leaf senescence( | + | 4. Overexpression of RLS1 displays a weak Phenotype of accelerated leaf senescence(figure3)leaves of RLS1-overexpressing plants senesced more rapidly than did |
| − | wild-type leaves. Individual leaves from wild-type plants became pale green after 4 d of dark treatment, whereas leaves from the RLS1-overexpressing plants showed severe yellowing. This was consistent with chlorophyll content of detached leaves during dark treatment<ref name="ref1" />[[File:RLS1.7.png|none|300px|''figure2 (from reference <ref name="ref1" />).'']][[File:RLS1.7A.png|none|300px | + | wild-type leaves. Individual leaves from wild-type plants became pale green after 4 d of dark treatment, whereas leaves from the RLS1-overexpressing plants showed severe yellowing. This was consistent with chlorophyll content of detached leaves during dark treatment<ref name="ref1" />[[File:RLS1.7.png|none|300px|''figure2 (from reference <ref name="ref1" />).'']][[File:RLS1.7A.png|none|300px]] (figure3)<ref name="ref1" /> |
===Evolution=== | ===Evolution=== | ||
| − | The putative NB domain of RLS1 contains the conserved motifs found in a large number of proteins binding ATP or GTP, and shows a significant similarity to that of homologous proteins from sorghum, grape, and black cottonwood. Moreover, it is also similar (23–30% similarity) to those of various NB-containing R proteins (Figure | + | 1.The putative NB domain of RLS1 contains the conserved motifs found in a large number of proteins binding ATP or GTP, and shows a significant similarity to that of homologous proteins from sorghum, grape, and black cottonwood. Moreover, it is also similar (23–30% similarity) to those of various NB-containing R proteins (Figure 4A). We then assessed the sequence diversity of the selected homologs, by generating a phylogenetic tree using the NB sequences (Figure 4B)The NB domains from 10 amino acids N-terminal to the first Gly in the Kinase 1a motif to 10 amino acids beyond the kinase 3amotif were used for analysis.Intriguingly, RLS1 was more closely related to the CC-NB-LRR proteins, Rx, I2, R3a (Moffett et al., 2002<ref name="ref3" />; Couch et al., 2006<ref name="ref4" />; Jia et al., 2010<ref name="ref5" />)than to TIR-NB-LRR proteins, N, RRS1-R, CHS3 (Deslandes et al., 2002<ref name="ref6" />; Konagaya et al., 2004<ref name="ref7" />; Yang et al., 2010<ref name="ref8" />).<ref name="ref1" />[[File:RLS1.5A.png|none|300px]][[File:RLS1.5B.png|none|300px]] (figure4) <ref name="ref1" /> |
| + | |||
| + | 2.The RLS1 locus was roughly mapped on chromosome 2. Subsequent finingmapping delimited the RLS1 locus to a 60-kb region between markers M17 and M24 (Figure 5A | ||
| + | and 5B). DNA sequencing analysis of the entire region in the rls1 mutant revealed a single C-to-T nucleotide substitution in the second exon of LOC_Os02g10900 (MSU Rice Genome Annotation Project: http://rice.plantbiology.msu.edu/), which results in Ser-to-Phe change at 994 residue (Figure 4C).<ref name="ref1" />[[File:RLS1.4.png|none|300px]] (figure5)<ref name="ref1" /> | ||
==Labs working on this gene== | ==Labs working on this gene== | ||
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<ref name="ref4"> Couch, B.C., Spangler, R., Ramos, C., and May, G. (2006). Pervasive purifying selection characterizes the evolution of I2 homologs. Mol. Plant–Microbe Interact. 19, 288–303.</ref> | <ref name="ref4"> Couch, B.C., Spangler, R., Ramos, C., and May, G. (2006). Pervasive purifying selection characterizes the evolution of I2 homologs. Mol. Plant–Microbe Interact. 19, 288–303.</ref> | ||
<ref name="ref5"> Jia, Z., Cui, Y., Li, Y.,Wang, X., Du, Y., and Huang, S. (2010). Inducible positive mutant screening system to unveil the signaling pathway of late blight resistance. J. Integr. Plant Biol. 52, 476–484.</ref> | <ref name="ref5"> Jia, Z., Cui, Y., Li, Y.,Wang, X., Du, Y., and Huang, S. (2010). Inducible positive mutant screening system to unveil the signaling pathway of late blight resistance. J. Integr. Plant Biol. 52, 476–484.</ref> | ||
| + | <ref name="ref6">Deslandes, L., Olivier, J., Theulieres, F., Hirsch, J., Feng, D.X., Bittner- Eddy, P., Beynon, J., and Marco, Y. (2002). Resistance to Ralstonia | ||
| + | solanacearum in Arabidopsis thaliana is conferred by the recessive RRS1-R gene, a member of a novel family of resistance genes. Proc. Natl Acad. Sci. U S A. 99, 2404–2409.</ref> | ||
| + | <ref name="ref7">Konagaya, K., Matsushita, Y., Kasahara, M., and Nyunoya, H.(2004). Members of 14–3–3 protein isoforms interacting with the resistance gene product N and the elicitor of tobacco mosaic virus. J. Gen. Plant Pathol. 70, 221–231.</ref> | ||
| + | <ref name="ref8">Yang, H., Shi, Y., Liu, J., Guo, L., Zhang, X., and Yang, S. (2010). A mutant CHS3 protein with TIR-NB-LRR-LIMdomains modulates growth, cell death and freezing tolerance in a temperaturedependent manner in Arabidopsis. Plant J. 63, 283–296.</ref> | ||
</references> | </references> | ||
==Structured Information== | ==Structured Information== | ||
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Latest revision as of 06:30, 14 May 2015
The RLS1 locus was roughly mapped on chromosome 2. And it encodes a previouslyuncharacterized NB (nucleotide-binding site)-containing protein with an ARM (armadillo) domain at the carboxyl terminus .Consistent with its involvement in leaf senescence, RLS1 was up-regulated during dark-induced leaf senescence and down-regulated by cytokinin. Intriguingly, constitutive expression of RLS1 also slightly accelerated leaf senescence with decreased chlorophyll content in transgenic rice plants.[1]
Contents
Annotated Information
Function
1.Map-based cloning of the RLS1 gene revealed that it encodes a previously uncharacterized NB (nucleotide-binding site)-containing protein with an ARM (armadillo) domain at the carboxyl terminus.The rls1 mutant displayed accelerated leaf senescence in both natural and dark-induced senescence, in comparison with the wild-type. We found that PCD involved in chloroplast degradation was misregulated in the leaf cells of rls1. Map-based cloning revealed that RLS1 encodes a novel NB containing protein with an ARM domain that presents only in sorghum, grape, and black cottonwood genomes.[1]
2.Consistent with its involvement in leaf senescence, RLS1 was up-regulated during dark-induced leaf senescence and down-regulated by cytokinin.[1]
3.Intriguingly, constitutive expression of RLS1 also slightly accelerated leaf senescence with decreased chlorophyll content in transgenic rice plants.The rls1 mutant plants showed accelerated leaf senescence under both natural and dark-induced conditions(Figure 1A, 1C, and 1D） . Therefore, the accelerated senescence of the rls1 mutant appears not to be directly induced by the formation of spontaneous lesions.The rapid loss of chlorophyll was the main cause of accelerated leaf senescence in rls1.[1]
4. The RLS1 gene might be involved in PCD that affects specific cellular processes.previously uncharacterized NB–ARM protein involved in PCD during plant growth and development, providing a unique tool for dissecting possible autophagymediated PCD during senescence in plants.[1]
5. RLS1 Is necessary for proper Chloroplast degradation.The mutation in the RLS1 accelerates the degradation of chloroplasts probably through an autophagy-mediated partial degradation process[1]
Expression
1.There is only one copy of the RLS1 gene in the rice genome. The RLS1 homolog genes with unknown function were only found in sorghum, grape, and black cottonwood by a BLAST search. The putative NB domain of RLS1 contains the conserved motifs found in a large number of proteins binding ATP or GTP, and shows a significant similarity to that of homologous proteins from sorghum, grape, and black cottonwood. Genetic studies have provided evidence that NB-containing R proteins in plant, such as RPS4, RPM1, can activate cell death during HR execution (Hofius et al., 2009[2]).[1]
2. RLS1 expression Is affected by dark-induced senescence and Cytokinin treatment. The expression of RLS1 was significantly induced in the seedlings transferred into darkness and reached the maximum level 12 h after treatment (Figure2). Accumulation of the RLS1 transcript was markedly reduced in the seedlings treated with 20 lM trans-zeatin (tZ) for 24 h (Figure1). These results suggested that RLS1 is involved in leaf senescence.[1]
3. The expression profile of RLS1 was investigated in various rice tissues at the adult stage with the quantitative real-time PCR approach. The results showed that RLS1 transcripts accumulated constitutively during leaf development, from young to senescent leaves (Figure 2). In addition, RLS1 was constitutively but weakly expressed in the root of seedling, panicle, and spikelet. The highest level of the RLS1 transcript was detected in mature leaves, consistent with the phenotype of rls1.[1]
4. Overexpression of RLS1 displays a weak Phenotype of accelerated leaf senescence(figure3)leaves of RLS1-overexpressing plants senesced more rapidly than did
wild-type leaves. Individual leaves from wild-type plants became pale green after 4 d of dark treatment, whereas leaves from the RLS1-overexpressing plants showed severe yellowing. This was consistent with chlorophyll content of detached leaves during dark treatment[1]![figure2 (from reference [1]).](https://ngdc.cncb.ac.cn/ricewiki/index.php/File:RLS1.7.png)
Evolution
1.The putative NB domain of RLS1 contains the conserved motifs found in a large number of proteins binding ATP or GTP, and shows a significant similarity to that of homologous proteins from sorghum, grape, and black cottonwood. Moreover, it is also similar (23–30% similarity) to those of various NB-containing R proteins (Figure 4A). We then assessed the sequence diversity of the selected homologs, by generating a phylogenetic tree using the NB sequences (Figure 4B)The NB domains from 10 amino acids N-terminal to the first Gly in the Kinase 1a motif to 10 amino acids beyond the kinase 3amotif were used for analysis.Intriguingly, RLS1 was more closely related to the CC-NB-LRR proteins, Rx, I2, R3a (Moffett et al., 2002[3]; Couch et al., 2006[4]; Jia et al., 2010[5])than to TIR-NB-LRR proteins, N, RRS1-R, CHS3 (Deslandes et al., 2002[6]; Konagaya et al., 2004[7]; Yang et al., 2010[8]).[1]
2.The RLS1 locus was roughly mapped on chromosome 2. Subsequent finingmapping delimited the RLS1 locus to a 60-kb region between markers M17 and M24 (Figure 5A
and 5B). DNA sequencing analysis of the entire region in the rls1 mutant revealed a single C-to-T nucleotide substitution in the second exon of LOC_Os02g10900 (MSU Rice Genome Annotation Project: http://rice.plantbiology.msu.edu/), which results in Ser-to-Phe change at 994 residue (Figure 4C).[1]
Labs working on this gene
1.National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China[1]
2.Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, China[1]
3. China National Rice Research Institute, Hangzhou 310006, China[1]
References
- ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 Bin-Bin Jiao;Jian-Jun Wang;Xu-Dong Zhu;Long-Jun Zeng;Qun Li;Zu-Hua He . A Novel Protein RLS1 with NB–ARM Domains Is Involved in Chloroplast Degradation during Leaf Senescence in Rice Molecular Plant, 2012, 5(1): 205-217
- ↑ Hofius, D., Schultz-Larsen, T., Joensen, J., Tsitsigiannis, D.I., Petersen, N.H., Mattsson, O., Jorgensen, L.B., Jones, J.D., Mundy, J., and Petersen, M. (2009). Autophagic components contribute to hypersensitive cell death in Arabidopsis. Cell. 137, 773–783.
- ↑ Moffett, P., Farnham, G., Peart, J., and Baulcombe, D.C. (2002). Interaction between domains of a plant NBS–LRR protein in disease resistance-related cell death. EMBO J. 21, 4511–4519.
- ↑ Couch, B.C., Spangler, R., Ramos, C., and May, G. (2006). Pervasive purifying selection characterizes the evolution of I2 homologs. Mol. Plant–Microbe Interact. 19, 288–303.
- ↑ Jia, Z., Cui, Y., Li, Y.,Wang, X., Du, Y., and Huang, S. (2010). Inducible positive mutant screening system to unveil the signaling pathway of late blight resistance. J. Integr. Plant Biol. 52, 476–484.
- ↑ Deslandes, L., Olivier, J., Theulieres, F., Hirsch, J., Feng, D.X., Bittner- Eddy, P., Beynon, J., and Marco, Y. (2002). Resistance to Ralstonia solanacearum in Arabidopsis thaliana is conferred by the recessive RRS1-R gene, a member of a novel family of resistance genes. Proc. Natl Acad. Sci. U S A. 99, 2404–2409.
- ↑ Konagaya, K., Matsushita, Y., Kasahara, M., and Nyunoya, H.(2004). Members of 14–3–3 protein isoforms interacting with the resistance gene product N and the elicitor of tobacco mosaic virus. J. Gen. Plant Pathol. 70, 221–231.
- ↑ Yang, H., Shi, Y., Liu, J., Guo, L., Zhang, X., and Yang, S. (2010). A mutant CHS3 protein with TIR-NB-LRR-LIMdomains modulates growth, cell death and freezing tolerance in a temperaturedependent manner in Arabidopsis. Plant J. 63, 283–296.
