Os01g0253300 - Revision history

Xysj2012: /* Structured Information */

2015-05-13T07:07:47Z

‎Structured Information

Jianchao Zhang: /* References */

2014-06-06T14:35:31Z

‎References

Jianchao Zhang: /* Knowledge Extension */

2014-06-06T14:34:41Z

‎Knowledge Extension

Jianchao Zhang: /* Evolution */

2014-06-06T14:33:47Z

‎Evolution

Ibpchenwenbo: /* References */

2014-06-06T14:18:09Z

‎References

Ibpchenwenbo: /* Protein structure */

2014-06-06T14:15:46Z

‎Protein structure

Ibpchenwenbo: /* Protein structure */

2014-06-06T14:15:22Z

‎Protein structure

Ibpchenwenbo: /* Protein structure */

2014-06-06T14:12:49Z

‎Protein structure

Ibpchenwenbo: /* Protein structure */

2014-06-06T14:12:20Z

‎Protein structure

Ibpchenwenbo: /* Evolution */

2014-06-06T14:08:23Z

‎Evolution

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

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 <ref name="ref6">
 Iwasaki T, Matsuki R, Shoji K, Sanmiya K, Miyao M, Yamamoto N. A novel importin alpha from rice, a component involved in the process of nuclear protein transport. FEBS Lett. 1998 May 29;428(3):259-62.</ref>
 </references>

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 ===Knowledge Extension===
-Rice encodes many kinds of  importin proteins such as importin α1a/1b,importinβand importin α1a is the most studied gene in rice with its crystal structure complex being resolved<ref name="ref5" /><ref name="ref5" />. Importin α1a functions as another importin α protein by form a complex with importin βand NLS-containing substrate.As shown in Figure -8, a single round of importin α-mediated import can be divided into six steps: (i) formation of a ternary complex in the cytoplasm; (ii) importin β-mediated binding of the ternary complex to docking sites at the periphery of the NPC; (iii) importin β-mediated translocation through the NPC; (iv) dissociation of the ternary complex, triggered, in part, by the binding of the small nuclear GTPase Ran–GTP to importin β; (v) recycling of importin α to the cytoplasm bound to the exportin CAS–Ran–GTP; and (vi) disassembly of the export complex and release of free importin α to the cytoplasm. Disassembly is induced by the Ran–GAP-induced hydrolysis of GTP by Ran. Ran–GDP and CAS are recycled back to the nucleus for further rounds of transport. Back in the nucleus, Ran–GDP is converted to Ran–GTP by the guanine nucleotide exchange factor RCC1.<ref name="ref5" />
+Rice encodes many kinds of  importin proteins such as importin α1a/1b,importinβand importin α1a is the most studied gene in rice with its crystal structure complex being resolved<ref name="ref5" /><ref name="ref7" />. Importin α1a functions as another importin α protein by form a complex with importin βand NLS-containing substrate.As shown in Figure -8, a single round of importin α-mediated import can be divided into six steps: (i) formation of a ternary complex in the cytoplasm; (ii) importin β-mediated binding of the ternary complex to docking sites at the periphery of the NPC; (iii) importin β-mediated translocation through the NPC; (iv) dissociation of the ternary complex, triggered, in part, by the binding of the small nuclear GTPase Ran–GTP to importin β; (v) recycling of importin α to the cytoplasm bound to the exportin CAS–Ran–GTP; and (vi) disassembly of the export complex and release of free importin α to the cytoplasm. Disassembly is induced by the Ran–GAP-induced hydrolysis of GTP by Ran. Ran–GDP and CAS are recycled back to the nucleus for further rounds of transport. Back in the nucleus, Ran–GDP is converted to Ran–GTP by the guanine nucleotide exchange factor RCC1.<ref name="ref5" />
 [[File:Fig-8 The nucleocytoplasmic shuttling cycle of importin α.png]]

← Older revision		Revision as of 14:33, 6 June 2014
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	Fig-7:(Phylogenetic tree of importinK. The tree was constructed by the UPGMA method using the GENETYX-MAC 7.3 software(Software Development Co., Tokyo) with default parameters. The accession number of the putative open reading frame T10M13.16 which is predicted ) From<ref name="ref6" />		Fig-7:(Phylogenetic tree of importinK. The tree was constructed by the UPGMA method using the GENETYX-MAC 7.3 software(Software Development Co., Tokyo) with default parameters. The accession number of the putative open reading frame T10M13.16 which is predicted ) From<ref name="ref6" />
		+
		+	===Knowledge Extension===
		+	Rice encodes many kinds of importin proteins such as importin α1a/1b,importinβand importin α1a is the most studied gene in rice with its crystal structure complex being resolved<ref name="ref5" /><ref name="ref5" />. Importin α1a functions as another importin α protein by form a complex with importin βand NLS-containing substrate.As shown in Figure -8, a single round of importin α-mediated import can be divided into six steps: (i) formation of a ternary complex in the cytoplasm; (ii) importin β-mediated binding of the ternary complex to docking sites at the periphery of the NPC; (iii) importin β-mediated translocation through the NPC; (iv) dissociation of the ternary complex, triggered, in part, by the binding of the small nuclear GTPase Ran–GTP to importin β; (v) recycling of importin α to the cytoplasm bound to the exportin CAS–Ran–GTP; and (vi) disassembly of the export complex and release of free importin α to the cytoplasm. Disassembly is induced by the Ran–GAP-induced hydrolysis of GTP by Ran. Ran–GDP and CAS are recycled back to the nucleus for further rounds of transport. Back in the nucleus, Ran–GDP is converted to Ran–GTP by the guanine nucleotide exchange factor RCC1.<ref name="ref5" />
		+
		+	[[File:Fig-8 The nucleocytoplasmic shuttling cycle of importin α.png]]
		+
		+	Fig-8:The nucleocytoplasmic shuttling cycle of importin α. (i) Importin α (α) forms a ternary complex with importin β (β) and cargo (blue circles). (ii) The ternary complex docks at the nuclear-pore complex (NPC) and (iii)translocates into the nucleus. (iv) Binding of Ran–GTP triggers the dissociation of the ternary complex. (v)Importin α binds to the exportin CAS–Ran–GTP complex and is exported to the cytoplasm. (vi) Ran–GAP-stimulated hydrolysis of GTP by Ran triggers the dissociation of the exportin complex and releases free importin α into the cytoplasm for another transport cycle. The recycling of importin β to the cytoplasm, and of Ran–GDP to the nucleus and its conversion to Ran–GTP are not shown.

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

@@ Line 57: / Line 57: @@
 <ref name="ref4">
 Shoji K, Iwasaki T, Matsuki R, Miyao M, Yamamoto N. Cloning of a cDNA encoding an importin-alpha and down-regulation of the gene by light in rice leaves. Gene. 1998 Jun 8;212(2):279-86.</ref>
+<ref name="ref5">
 <ref name="ref6">
 Iwasaki T, Matsuki R, Shoji K, Sanmiya K, Miyao M, Yamamoto N. A novel importin alpha from rice, a component involved in the process of nuclear protein transport. FEBS Lett. 1998 May 29;428(3):259-62.</ref>

← Older revision		Revision as of 14:15, 6 June 2014
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	2.The crystal structures of their complexes with rice importin alpha-1a show that they bind to the minor NLS binding site[Fig6A]. By contrast, the crystal structures of their complexes with mouse (Mus musculus) importin alpha-1ashow preferential binding to the major NLS binding site[Fig6B]. The results reveal the molecular basis of a number of features of the classical nuclear transport pathway specific to plants<ref name="ref5" />.		2.The crystal structures of their complexes with rice importin alpha-1a show that they bind to the minor NLS binding site[Fig6A]. By contrast, the crystal structures of their complexes with mouse (Mus musculus) importin alpha-1ashow preferential binding to the major NLS binding site[Fig6B]. The results reveal the molecular basis of a number of features of the classical nuclear transport pathway specific to plants<ref name="ref5" />.
		+
	[[File:Fig 6 structure difference.jpg]]		[[File:Fig 6 structure difference.jpg]]

← Older revision		Revision as of 14:12, 6 June 2014
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	Fig-5:crystal structure of importin alpha-1a.From ref<ref name="ref5" />		Fig-5:crystal structure of importin alpha-1a.From ref<ref name="ref5" />
		+
	2.The crystal structures of their complexes with rice importin alpha-1a show that they bind to the minor NLS binding site[Fig6A]. By contrast, the crystal structures of their complexes with mouse (Mus musculus) importin alpha-1ashow preferential binding to the major NLS binding site[Fig6B]. The results reveal the molecular basis of a number of features of the classical nuclear transport pathway specific to plants<ref name="ref5" />.		2.The crystal structures of their complexes with rice importin alpha-1a show that they bind to the minor NLS binding site[Fig6A]. By contrast, the crystal structures of their complexes with mouse (Mus musculus) importin alpha-1ashow preferential binding to the major NLS binding site[Fig6B]. The results reveal the molecular basis of a number of features of the classical nuclear transport pathway specific to plants<ref name="ref5" />.

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 ===Protein structure===
 .The structure of rice importin alpha-1a  comprises 10 ARM repeats (green, cartoon representation) and two NLS-like sequences from the N-terminal IBB domain(shown in yellow stick )[FIG-5]<ref name="ref5" />.
 .The crystal structures of their complexes with rice importin alpha-1a show that they bind to the minor NLS binding site[Fig6A]. By contrast, the crystal structures of their complexes with mouse (Mus musculus) importin alpha-1ashow preferential binding to the major NLS binding site[Fig6B]. The results reveal the molecular basis of a number of features of the classical nuclear transport pathway specific to plants<ref name="ref5" />.
 ===Evolution===
 The phylogenetic tree of importin alpha shows that the rice importin alpha-1a protein is the most distant member from various organisms[Fig-7]<ref name="ref6" />.we could find another EST from Arabidopsis (accession number F15465), which has about 60% identity with #61L at the levelof both nucleotide and amino acid sequences. It might be interpreted that importin alpha-1a homologous to rice #61L(Refere to importin alpha-1a) is also present in Arabidopsis, and that the #61L protein and the homologue are functionally differentiated from the known importin alpha-1a.