Os03g0123300 - Revision history

Xysj2017: /* Phenotypic analysis */

2017-02-14T02:07:07Z

‎Phenotypic analysis

Xysj2017: /* Phenotypic analysis */

2017-02-14T02:06:03Z

‎Phenotypic analysis

Xysj2017 at 02:04, 14 February 2017

2017-02-14T02:04:15Z

Rice2012: /* Structured Information */

2015-06-12T05:00:50Z

‎Structured Information

EmmaJune: /* Annotated Information */

2014-06-09T13:48:05Z

‎Annotated Information

EmmaJune: /* Annotated Information */

2014-06-09T13:47:28Z

‎Annotated Information

EmmaJune: /* References */

2014-06-09T08:24:05Z

‎References

EmmaJune: /* References */

2014-06-09T08:21:58Z

‎References

Somnussunshine: /* Function */

2014-06-09T06:13:33Z

‎Function

Somnussunshine: /* Function */

2014-06-09T02:40:02Z

‎Function

@@ Line 11: / Line 11: @@
 ===Phenotypic analysis===
 * The rice tiller enhancer (te) mutant displays a drastically increased tiller number.
-[[File:214-Os03g0123300.png|center|thumb|800px|'''Figure 1.''' ''Phenotype characterization of te mutant and map-based cloning of TE.(a) Phenotype of WT and te plants at the seventh leaf stage. (b) Phenotype of WT and te plants at the heading stage. (c) WT produces un-elongated lateral bud (left panel, arrowhead) on the elongated upper internodes, whereas te mutant produces additional tillers (right panel, arrowhead) from the elongated internodes. (d) Tiller number comparison between WT (blue) and te (red) plants at the heading stage. TTs, total tillers; LTs, lower node tillers; HTs, higher node tillers. LTs are the tillers outgrown from the un-elongated basal internodes. HTs are the tillers outgrown from the elongated internodes.<ref name="ref1" />.'']]
+<br>
 ===Expression===

@@ Line 11: / Line 11: @@
 ===Phenotypic analysis===
 * The rice tiller enhancer (te) mutant displays a drastically increased tiller number.
 ===Expression===

@@ Line 1: / Line 1: @@
-Please input one-sentence summary here.
+The rice '''''Os03g0123300''''' was reported as '''''TE''''' in 2012 <ref name="ref1" /> by researchers from China.
 ==Annotated Information==
 ===Function===
-'''''Tillering and Dwarf 1'''''('''''TAD1'''''), which encodes a co-activator of the anaphase-promoting complex (APC/C), a multi-subunit E3 ligase. The protein interacts with moC1, forms a complex with osAPC10 and functions as a co-activator of APC/C to target MoC1 for degradation in a cell-cycle-dependent manner.
+* '''''TE''''' encodes a rice homologue of Cdh1, and that TE acts as an activator of the anaphase promoting complex/cyclosome (APC/C) complex
+* Besides having a conserved role in regulating cell cycle, APC/C TE has a unique function in regulating the plant-specific postembryonic shoot branching and tillering, which are major determinants of plant architecture and grain yield.
-OsAPC10 interacts with TAD1 in vivo and their interaction occurs in the nucleus of rice protoplasts. Coexpressed TAD1, MOC1 and OsAPC10 proteins in the rice protoplasts can prove that MOC1 can indeed form a  protein complex with TAD1 and OsAPC10 in vivo(Fig.b). Therefore, it is very likely that TAD1 recruits MOC1 to APC/C, and OsAPC10 is also involved in recognizing and targeting MOC1 for further degradation.
+===Phenotypic analysis===
-TAD1 may recruit MOC1 to APC/C for degradation mainly at the G1-phase Cell division may execute the activation of bud cells. The activity of cell division blocked in the G1-phase possibly accompanies low levels of MOC1 proteins  in  the  dormant  tiller  buds. Based on the cellcycle profile of bud cells and the function of APC/C TAD1–MOC1, it can be proposed that the APC/CTAD1–MOC1 complex may act locally in tiller buds. During the cell-cycle progression of tiller bud cells, TAD1 is activated in the G1-phase, where it targets MOC1 for degradation to maintain a low level of MOC1. When tiller cells transit into the next phase, the TAD1 level is reduced, which causes MOC1 to accumulate and regain its function in controlling tillering.
+* The rice tiller enhancer (te) mutant displays a drastically increased tiller number.
 ===Expression===
+* TE coexpresses with MOC1 in the axil of leaves, where the APC/C TE complex mediates the degradation of MOC1 by the ubiquitin–26S proteasome pathway, and consequently downregulates the expression of the meristem identity gene Oryza sativa homeobox 1, thus repressing axillary meristem initiation and formation.
 ==References==
-Cao Xu;Yonghong Wang;Yanchun Yu;Jingbo Duan;Zhigang Liao;Guosheng Xiong;Xiangbing Meng;Guifu Liu;Qian Qian;Jiayang Li.Degradation of MONOCULM 1 by APC/CTAD1 regulates rice tillering.Nature Communications, 2012, 3: 750
+<references>
+* <ref name="ref1">
-Stegmuller, J. et al.Cell-intrinsic regulation of axonal morphogenesis by the Cdh1-APC target SnoN. Neuron 50,389–400 (2006).
+Lin Q, Wang D, Dong H, Gu S, Cheng Z, Gong J, Qin R, Jiang L, Li G, Wang JL,
+Wu F, Guo X, Zhang X, Lei C, Wang H, Wan J. Rice APC/C(TE) controls tillering by
-Lasorella, A. et al.Degradation of Id2 by the anaphase-promoting complex couples cell cycle exit and axonal growth. Nature 442,471–474 (2006).
+mediating the degradation of MONOCULM 1. Nat Commun. 2012 Mar 20;3:752. doi:
+.1038/ncomms1716. PubMed PMID: 22434195; PubMed Central PMCID: PMC3316886.
 ==Labs working on this gene==
-State Key Laboratory of Plant Genomics and National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China. State Key Laboratory of Rice Biology, China National Rice Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou 310006, China. College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
+* National Key Facility for Crop Gene Resources and Genetic Improvement, Institute of Crop Science, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
 ==Structured Information==

@@ Line 39: / Line 39: @@
 ==Structured Information==
 [[Category:Genes]]
 [[Category:Japonica mRNA]]

@@ Line 23: / Line 23: @@
                             Expression of TAD1 during the cell-cycle progression and phenotypes of ''TAD1''-overexpressing transgenic plants.
+''TAD1'' has an oscillated expression pattern during the cell-cycle progression, showing a higher level in the G1-phase and a lower level in the S- and G2/M-phases. The  overexpression  of MOC1 resulted in similar phenotypes to that of the tad1mutant plant, such as more tillers and reduced  plant  height, whereas TAD1-overexpressing transgenic plants showed a reduced tiller number,a similar phenotype to ''moc1''.Real-time PCR analysis showed that ''TAD1''is expressed ubiquitously in the examined rice organs, including roots, shoot apices, axillary buds, internodes, nodes, and young leaves  and  panicles, but more abundant in young  leaves, axillary buds and nodes.The tissue-specific expression pattern of ''TAD1'' was further examined by messenger RNA in situhybridization. ''TAD1'' was predominantly expressed in the leaf primordia and young leaves, tiller buds, inflorescence promordia, and crown root promordia. In addition, ''TAD1'' expression was detected in vascular bundles at the unenlongated stem.
 ===Evolution===

← Older revision		Revision as of 08:24, 9 June 2014
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	==References==		==References==
		+	Cao Xu;Yonghong Wang;Yanchun Yu;Jingbo Duan;Zhigang Liao;Guosheng Xiong;Xiangbing Meng;Guifu Liu;Qian Qian;Jiayang Li.Degradation of MONOCULM 1 by APC/CTAD1 regulates rice tillering.Nature Communications, 2012, 3: 750
		+
		+	Stegmuller, J. et al.Cell-intrinsic regulation of axonal morphogenesis by the Cdh1-APC target SnoN. Neuron 50,389–400 (2006).
		+
		+	Lasorella, A. et al.Degradation of Id2 by the anaphase-promoting complex couples cell cycle exit and axonal growth. Nature 442,471–474 (2006).

	==Labs working on this gene==		==Labs working on this gene==

← Older revision		Revision as of 08:21, 9 June 2014
Line 29:		Line 29:

	==References==		==References==
−	Cao Xu;Yonghong Wang;Yanchun Yu;Jingbo Duan;Zhigang Liao;Guosheng Xiong;Xiangbing Meng;Guifu Liu;Qian Qian;Jiayang Li.Degradation of MONOCULM 1 by APC/CTAD1 regulates rice tillering.Nature Communications, 2012, 3: 750
−	~~Stegmuller, J. et al.Cell-intrinsic regulation of axonal morphogenesis by the Cdh1-APC target SnoN. Neuron 50,389–400 (2006).~~
−	~~Lasorella, A. et al.Degradation of Id2 by the anaphase-promoting complex couples cell cycle exit and axonal growth. Nature 442,471–474 (2006).~~

	==Labs working on this gene==		==Labs working on this gene==

@@ Line 5: / Line 5: @@
 '''''Tillering and Dwarf 1'''''('''''TAD1'''''), which encodes a co-activator of the anaphase-promoting complex (APC/C), a multi-subunit E3 ligase. The protein interacts with moC1, forms a complex with osAPC10 and functions as a co-activator of APC/C to target MoC1 for degradation in a cell-cycle-dependent manner.
-''TAD1'' encodes a Cdh1-type activator of  APC/C, an ortholog to CCS52A in dicots.During the cell-cycl progression, ''TAD1'' shows an oscillating expression  pattern with a higher level in the G1-phase.The ''TAD1''-deduced amino-acid sequence contains several conserved domains, including seven WD repeats, C-box, CSM, RVL and IR motifs.
+''TAD1'' encodes a Cdh1-type activator of  APC/C, an ortholog to CCS52A in dicots.During the cell-cycl progression, ''TAD1'' shows an oscillating expression  pattern with a higher level in the G1-phase.The ''TAD1''-deduced amino-acid sequence contains several conserved domains, including seven WD repeats, C-box, CSM, RVL and IR motifs.Along with APC/C, they form APC/C-TAD1complex and functions as a key regulator of tillering.TAD1 can specifically recruit MOC1 by interacting with OsAPC10 and then degrade MOC1 to maintain an appropriate protein level of MOC1 to control rice tillering. In the absence of TAD1 function, MOC1 fails to be recruited to the APC/C for degradation, resulting in an accumulation of endogenous MOC1 proteins and thus an increase in tiller number in the tad1mutant plant.
                                           [[File:Deternination_of_the_interaction_between_TAD1_and_MOC1_by_coimmunoprecipitation_and_BiFC_assays.png]]
                                                    Deternination of the interaction between TAD1 and MOC1 by coimmunoprecipitation and BiFC assays.
-Sequence analysis revealed that MOC1 harbours a typical D-box at the N-terminal  (Fig.a). Therefore, it is very likely that MOC1 and TAD1 directly interact to control rice tillering. MOC1–GFP fusion protein could capture the TAD1–FLAG fusion protein, suggesting an in vivo interaction between MOC1 and TAD1 (Fig.b). Bimolecular fluorescence complementation shown in Fig.c, when the full-length cDNAs of ''TAD1'' and ''MOC1'' were introduced into rice protoplasts simultaneously, the fluorescence signal was detected in the nucleus, indicating that TAD1 can directly interact with MOC1 in the nucleus. Furthermore, when  two conserved  residues, arginine  and leucine, of the D-box at the  N-terminal were changed  into alanine  (Fig.a),  the ''MOC1'' protein was unable to interact with TAD1, demonstrating that the D-box is indispensable  for  the  interaction  between  MOC1 and TAD1 (Fig.c). In addition, a series of truncated ''TAD1'' proteins were generated to determine the domains that are essential for the interaction with MOC1 via the BiFC analysis (Fig.d). The results showed that the N-terminal 203 amino acids of TAD1 are sufficient to interact with MOC1.
+Sequence analysis revealed that MOC1 harbours a typical D-box at the N-terminal  (Fig.a). Therefore, it is very likely that MOC1 and TAD1 directly interact to control rice tillering. MOC1–GFP fusion protein could capture the TAD1–FLAG fusion protein, suggesting an in vivo interaction between MOC1 and TAD1 (Fig.b). Bimolecular fluorescence complementation shown in Fig.c, when the full-length cDNAs of ''TAD1'' and ''MOC1'' were introduced into rice protoplasts simultaneously, the fluorescence signal was detected in the nucleus, indicating that TAD1 can directly interact with MOC1 in the nucleus. Furthermore, when  two conserved  residues, arginine  and leucine, of the D-box at the N-terminal were changed  into alanine  (Fig.a),  the ''MOC1'' protein was unable to interact with TAD1, demonstrating that the D-box is indispensable for the interaction between  MOC1 and TAD1 (Fig.c). In addition, a series of truncated ''TAD1'' proteins were generated to determine the domains that are essential for the interaction with MOC1 via the BiFC analysis (Fig.d). The results showed that the N-terminal 203 amino acids of TAD1 are sufficient to interact with MOC1.
                                                   [[File:The_APC_C(TAD1)_complex-mediated_degradation_of_MOC1.png]]
                                                       The APC C(TAD1) complex-mediated degradation of MOC1.
-OsAPC10 interacts with TAD1 in vivo and their interaction occurs in the nucleus of rice protoplasts. Coexpressed TAD1, MOC1 and OsAPC10 proteins in the rice protoplasts can prove that MOC1 can  indeed form a  protein complex with TAD1 and OsAPC10 in vivo(Fig.b). Therefore, it is very likely that TAD1 recruits MOC1 to APC/C, and OsAPC10 is also involved in recognizing and targeting MOC1 for further degradation.
+OsAPC10 interacts with TAD1 in vivo and their interaction occurs in the nucleus of rice protoplasts. Coexpressed TAD1, MOC1 and OsAPC10 proteins in the rice protoplasts can prove that MOC1 can indeed form a  protein complex with TAD1 and OsAPC10 in vivo(Fig.b). Therefore, it is very likely that TAD1 recruits MOC1 to APC/C, and OsAPC10 is also involved in recognizing and targeting MOC1 for further degradation.
-TAD1 may recruit MOC1 to APC/C for degradation mainly at the G1-phase Cell division may execute the activation of bud cells. The activity of cell division blocked in the G1-phase possibly accompanies low levels of  MOC1  proteins  in  the  dormant  tiller  buds.  Based  on  the  cellcycle profile of bud cells and the function of APC/C TAD1–MOC1, we propose that the APC/CTAD1–MOC1 complex may act locally in tiller buds. During the cell-cycle progression of tiller bud cells, TAD1 is activated in the G1-phase, where it targets MOC1 for degradation to maintain a low level of MOC1. When tiller cells transit into the next phase, the TAD1 level is reduced, which causes MOC1 to accumulate and regain its function in controlling tillering.
+TAD1 may recruit MOC1 to APC/C for degradation mainly at the G1-phase Cell division may execute the activation of bud cells. The activity of cell division blocked in the G1-phase possibly accompanies low levels of MOC1 proteins  in  the  dormant  tiller  buds. Based on the cellcycle profile of bud cells and the function of APC/C TAD1–MOC1, it can be proposed that the APC/CTAD1–MOC1 complex may act locally in tiller buds. During the cell-cycle progression of tiller bud cells, TAD1 is activated in the G1-phase, where it targets MOC1 for degradation to maintain a low level of MOC1. When tiller cells transit into the next phase, the TAD1 level is reduced, which causes MOC1 to accumulate and regain its function in controlling tillering.
 ===Expression===

← Older revision		Revision as of 02:40, 9 June 2014
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	[[File:The_APC_C(TAD1)_complex-mediated_degradation_of_MOC1.png]]		[[File:The_APC_C(TAD1)_complex-mediated_degradation_of_MOC1.png]]
		+	The APC C(TAD1) complex-mediated degradation of MOC1.

	OsAPC10 interacts with TAD1 in vivo and their interaction occurs in the nucleus of rice protoplasts. Coexpressed TAD1, MOC1 and OsAPC10 proteins in the rice protoplasts can prove that MOC1 can indeed form a protein complex with TAD1 and OsAPC10 in vivo(Fig.b). Therefore, it is very likely that TAD1 recruits MOC1 to APC/C, and OsAPC10 is also involved in recognizing and targeting MOC1 for further degradation.		OsAPC10 interacts with TAD1 in vivo and their interaction occurs in the nucleus of rice protoplasts. Coexpressed TAD1, MOC1 and OsAPC10 proteins in the rice protoplasts can prove that MOC1 can indeed form a protein complex with TAD1 and OsAPC10 in vivo(Fig.b). Therefore, it is very likely that TAD1 recruits MOC1 to APC/C, and OsAPC10 is also involved in recognizing and targeting MOC1 for further degradation.