Os02g0606700 - Revision history

Xysj2012: /* Structured Information */

2015-05-14T05:44:54Z

‎Structured Information

Xysj2012: /* References */

2014-06-04T09:49:17Z

‎References

Ximenchuixue at 02:42, 27 May 2014

2014-05-27T02:42:34Z

Ximenchuixue at 02:35, 27 May 2014

2014-05-27T02:35:30Z

Ximenchuixue at 02:34, 27 May 2014

2014-05-27T02:34:11Z

Ximenchuixue at 02:31, 27 May 2014

2014-05-27T02:31:55Z

Ximenchuixue at 02:31, 27 May 2014

2014-05-27T02:31:01Z

Ximenchuixue at 15:25, 19 May 2014

2014-05-19T15:25:27Z

Ximenchuixue at 15:21, 19 May 2014

2014-05-19T15:21:40Z

Ximenchuixue at 15:15, 19 May 2014

2014-05-19T15:15:47Z

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 ==Structured Information==
 [[Category:Genes]]
 [[Category:Japonica mRNA]]

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 <ref name="ref7"> Odegard W, Liu J J, de Lumen B O. Cloning and expression of rice (< i> Oryza sativa</i>) sucrose synthase 1 (RSs1) in developing seed endosperm[J]. Plant Science, 1996, 113(1): 67-78</ref>
-<references>
+</references>
 ==Structured Information==

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 <ref name="ref6"> 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).</ref>
 <ref name="ref7"> Odegard W, Liu J J, de Lumen B O. Cloning and expression of rice (< i> Oryza sativa</i>) sucrose synthase 1 (RSs1) in developing seed endosperm[J]. Plant Science, 1996, 113(1): 67-78</ref>
 <references>
-<ref name="ref8"> Ogawa D, Morita H, Hattori T, et al. Molecular characterization of the rice protein RSS1 required for meristematic activity under stressful conditions[J]. Plant Physiology and Biochemistry, 2012, 61: 54-60.
 ==Structured Information==
 {{JaponicaGene|

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 In addition to the N-terminal region containing the DEN-box and D-box/D-box-like motifs (region I), these RSS1 homologues have a well-conserved region in the middle region (region II), which includes a sequence (W–A–K/R–D/E/G–G–V/I–E) designated the ‘WAGE’ motif and a moderately conserved carboxyterminal acidic region (region III)and Supplementary . Notably, no proteins with overall similarity to RSS1 exist in eudicots, although sequences related to region I are found<ref name="ref1" />.
 ===Knowledge Extension===
-Post embryonic growth of plants depends on cell division activity in the shoot and root meristems, in conjunction with subsequent cell differentiation. Under environmental stress conditions, where plant growth is moderately impaired, the meristematic activity is maintained by mechanisms as yet unknown. We previously showed that the rice protein RSS1, whose stability is regulated depending on the cell cycle phases, is a key factor for the maintenance of meristematic activity under stressful conditions. RSS1 interacts with a catalytic subunit of protein phosphatase 1 (PP1), but other molecular characteristics are largely unknown. Here we show that RSS1 interacts with all the PP1 expressed in the shoot apex of rice. This interaction requires one of the conserved regions of RSS1, which is important for RSS1 function. Interestingly, the recombinant RSS1 protein is highly resistant to heat with respect to its anti-coagulability and binding activity to PP1. The features of RSS1 are reminiscent of those of inhibitor-2 of animals, although it is likely that the mode of function of RSS1 is different from that of inhibitor-2. Noticeably, RSS1 binds to PP1 under extremely high ionic strength conditions in vitro. Therefore, RSS1 possibly functions by forming a stable complex with PP1.<ref name="ref8" />
+Post embryonic growth of plants depends on cell division activity in the shoot and root meristems, in conjunction with subsequent cell differentiation. Under environmental stress conditions, where plant growth is moderately impaired, the meristematic activity is maintained by mechanisms as yet unknown. We previously showed that the rice protein RSS1, whose stability is regulated depending on the cell cycle phases, is a key factor for the maintenance of meristematic activity under stressful conditions. RSS1 interacts with a catalytic subunit of protein phosphatase 1 (PP1), but other molecular characteristics are largely unknown. Here we show that RSS1 interacts with all the PP1 expressed in the shoot apex of rice. This interaction requires one of the conserved regions of RSS1, which is important for RSS1 function. Interestingly, the recombinant RSS1 protein is highly resistant to heat with respect to its anti-coagulability and binding activity to PP1. The features of RSS1 are reminiscent of those of inhibitor-2 of animals, although it is likely that the mode of function of RSS1 is different from that of inhibitor-2. Noticeably, RSS1 binds to PP1 under extremely high ionic strength conditions in vitro. Therefore, RSS1 possibly functions by forming a stable complex with PP1.<ref name="ref8" />.
 ===Labs working on this gene===
@@ Line 51: / Line 51: @@
 <ref name="ref7"> Odegard W, Liu J J, de Lumen B O. Cloning and expression of rice (< i> Oryza sativa</i>) sucrose synthase 1 (RSs1) in developing seed endosperm[J]. Plant Science, 1996, 113(1): 67-78</ref>
 <references>
-<ref name="ref8">. Ogawa D, Morita H, Hattori T, et al. Molecular characterization of the rice protein RSS1 required for meristematic activity under stressful conditions[J]. Plant Physiology and Biochemistry, 2012, 61: 54-60.
+<ref name="ref8"> Ogawa D, Morita H, Hattori T, et al. Molecular characterization of the rice protein RSS1 required for meristematic activity under stressful conditions[J]. Plant Physiology and Biochemistry, 2012, 61: 54-60.
 ==Structured Information==
 {{JaponicaGene|

@@ Line 51: / Line 51: @@
 <ref name="ref7"> Odegard W, Liu J J, de Lumen B O. Cloning and expression of rice (< i> Oryza sativa</i>) sucrose synthase 1 (RSs1) in developing seed endosperm[J]. Plant Science, 1996, 113(1): 67-78</ref>
 <references>
-<ref name="ref8">. Daisuke Ogawa;Kiyomi Abe;Akio Miyao;Mikiko Kojima;Hitoshi Sakakibara;Megumi Mizutani;Haruka Morita;Yosuke Toda;Tokunori Hobo;Yutaka Sato;Tsukaho Hattori;Hirohiko Hirochika;Shin Takeda  RSS1 regulates the cell cycle and maintains meristematic activity under stress conditions in rice
+<ref name="ref8">. Ogawa D, Morita H, Hattori T, et al. Molecular characterization of the rice protein RSS1 required for meristematic activity under stressful conditions[J]. Plant Physiology and Biochemistry, 2012, 61: 54-60.
 ==Structured Information==
 {{JaponicaGene|

@@ Line 6: / Line 6: @@
 RSS1 ensures cell division activity under stress conditions<ref name="ref1" />.RSS1 affects SAM maintenance and abiotic stress responses<ref name="ref1" />.RSS1 contributes to maintenance of active cytokinin levels<ref name="ref1" />. In the shoot, RSS1 contributes to the maintenance of the SAM.
-we can see the size under stress conditions.See fig1<ref name="ref1" />. In agreement with the proposed function of RSS1, genes involved in the cell cycle and DNA replication are preferentially downregulated in rss1 under high-salt conditions. Conspicuously, more than 30% of the genes that are expressed specifically in the shoot apex are coordinately downregulated in rss1 under high-salt conditions , supporting the proposed function of RSS1 in maintaining proliferative tissue activity<ref name="ref1" />. 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<ref name="ref2-6" />. What is more RSS1 acts as a key factor in the maintenance of meristematic activity by ensuring cell division under stressful environmental conditions<ref name="ref1" />.
+we can see the size under stress conditions.See fig1<ref name="ref1" />. In agreement with the proposed function of RSS1, genes involved in the cell cycle and DNA replication are preferentially downregulated in rss1 under high-salt conditions. Conspicuously, more than 30% of the genes that are expressed specifically in the shoot apex are coordinately downregulated in rss1 under high-salt conditions , supporting the proposed function of RSS1 in maintaining proliferative tissue activity<ref name="ref1" />. 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<ref name="ref2" /><ref name="ref3" /><ref name="ref4" /><ref name="ref5" /><ref name="ref6" />. What is more RSS1 acts as a key factor in the maintenance of meristematic activity by ensuring cell division under stressful environmental conditions<ref name="ref1" />.
 ===Expression===

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 RSS1 ensures cell division activity under stress conditions<ref name="ref1" />.RSS1 affects SAM maintenance and abiotic stress responses<ref name="ref1" />.RSS1 contributes to maintenance of active cytokinin levels<ref name="ref1" />. In the shoot, RSS1 contributes to the maintenance of the SAM.
-we can see the size under stress conditions.See fig1[1]. In agreement with the proposed function of RSS1, genes involved in the cell cycle and DNA replication are preferentially downregulated in rss1 under high-salt conditions. Conspicuously, more than 30% of the genes that are expressed specifically in the shoot apex are 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]. What is more RSS1 acts as a key factor in the maintenance of meristematic activity by ensuring cell division under stressful environmental conditions[1].
+we can see the size under stress conditions.See fig1<ref name="ref1" />. In agreement with the proposed function of RSS1, genes involved in the cell cycle and DNA replication are preferentially downregulated in rss1 under high-salt conditions. Conspicuously, more than 30% of the genes that are expressed specifically in the shoot apex are coordinately downregulated in rss1 under high-salt conditions , supporting the proposed function of RSS1 in maintaining proliferative tissue activity<ref name="ref1" />. 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<ref name="ref2-6" />. What is more RSS1 acts as a key factor in the maintenance of meristematic activity by ensuring cell division under stressful environmental conditions<ref name="ref1" />.
 ===Expression===
 [[File:zzb.jpg|right|thumb|220px|'''Figure 2. <ref name="ref1" />.'']]
-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 is upregulated by low temperatures, but not by high-salt conditions Supplementary[1].In the shoot apical meristem (SAM), RSS1 mRNA is detected only weakly in the central zone, where the cells are less active in terms of division and are completely undifferentiated[1].People have established the spatial pression of RSsl in rice and found it to be expressed predominantly in the seed endosperm.Temporal expression analysis revealed maximum expression of seed development at 3-5DAP[7].Look at Fig 2.
+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 is upregulated by low temperatures, but not by high-salt conditions Supplementary<ref name="ref1" />.In the shoot apical meristem (SAM), RSS1 mRNA is detected only weakly in the central zone, where the cells are less active in terms of division and are completely undifferentiated<ref name="ref1" />.People have established the spatial pression of RSsl in rice and found it to be expressed predominantly in the seed endosperm.Temporal expression analysis revealed maximum expression of seed development at 3-5DAP<ref name="ref7" />.Look at Fig 2.
-These effects of RSS1 are exerted by regulating the G1–S transition, possibly through an interaction of RSS1 with protein phosphatase 1, and are mediated by the phytohormone, cytokinin[1].
+These effects of RSS1 are exerted by regulating the G1–S transition, possibly through an interaction of RSS1 with protein phosphatase 1, and are mediated by the phytohormone, cytokinin<ref name="ref1" />.
 ===Evolution===
 [[File:aaa.jpg|right|thumb|220px|'''Figure 3. <ref name="ref1" />.'']]
-RSS1-related sequences are not only highly conserved among monocots, but can also be identified in basal angiosperms, including Amborella trichopoda, which belongs to the most ancient lineage of extant angiosperms (Fig.3)22. RSS1-related genes also exist in gymnosperms, ferns and mosses[1].Please see Fig3.
+RSS1-related sequences are not only highly conserved among monocots, but can also be identified in basal angiosperms, including Amborella trichopoda, which belongs to the most ancient lineage of extant angiosperms (Fig.3)22. RSS1-related genes also exist in gymnosperms, ferns and mosses<ref name="ref1" />.Please see Fig3.
-In addition to the N-terminal region containing the DEN-box and D-box/D-box-like motifs (region I), these RSS1 homologues have a well-conserved region in the middle region (region II), which includes a sequence (W–A–K/R–D/E/G–G–V/I–E) designated the ‘WAGE’ motif and a moderately conserved carboxyterminal acidic region (region III)and Supplementary . Notably, no proteins with overall similarity to RSS1 exist in eudicots, although sequences related to region I are found[1].
+In addition to the N-terminal region containing the DEN-box and D-box/D-box-like motifs (region I), these RSS1 homologues have a well-conserved region in the middle region (region II), which includes a sequence (W–A–K/R–D/E/G–G–V/I–E) designated the ‘WAGE’ motif and a moderately conserved carboxyterminal acidic region (region III)and Supplementary . Notably, no proteins with overall similarity to RSS1 exist in eudicots, although sequences related to region I are found<ref name="ref1" />.
 ===Labs working on this gene===

@@ Line 4: / Line 4: @@
 ===Function===
 [[File:abc.jpg|right|thumb|220px|'''Figure 1. <ref name="ref1" />.'']]
-RSS1 ensures cell division activity under stress conditions[1].RSS1 affects SAM maintenance and abiotic stress responses[1].RSS1 contributes to maintenance of active cytokinin levels[1]. In the shoot, RSS1 contributes to the maintenance of the SAM.
+RSS1 ensures cell division activity under stress conditions<ref name="ref1" />.RSS1 affects SAM maintenance and abiotic stress responses<ref name="ref1" />.RSS1 contributes to maintenance of active cytokinin levels<ref name="ref1" />. In the shoot, RSS1 contributes to the maintenance of the SAM.
 we can see the size under stress conditions.See fig1[1]. In agreement with the proposed function of RSS1, genes involved in the cell cycle and DNA replication are preferentially downregulated in rss1 under high-salt conditions. Conspicuously, more than 30% of the genes that are expressed specifically in the shoot apex are 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]. What is more RSS1 acts as a key factor in the maintenance of meristematic activity by ensuring cell division under stressful environmental conditions[1].