Os04g0271200 - Revision history

Shfengna: /* Expression */

2014-06-10T08:01:06Z

‎Expression

Shfengna: /* Expression */

2014-06-10T07:59:52Z

‎Expression

Shfengna: /* Expression */

2014-06-10T07:58:08Z

‎Expression

Shfengna: /* Function */

2014-06-10T07:50:42Z

‎Function

Shfengna: /* Function */

2014-06-10T07:47:56Z

‎Function

Lina: /* References */

2014-06-10T07:32:58Z

‎References

Lina: /* Evolution */

2014-06-10T07:26:33Z

‎Evolution

Lina: /* Evolution */

2014-06-10T07:20:28Z

‎Evolution

Shfengna: /* Expression */

2014-06-08T09:32:51Z

‎Expression

Shfengna: /* Expression */

2014-06-08T09:32:34Z

‎Expression

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 [[File:1-s2.0-S0006291X09015459-gr1.jpg|left|thumb|360px|1-s2.0-S0006291X09015459-gr1.''<ref name="ref2" />'']]
 <br />Expression analysis of the rice HDAC genes. Upper: A hierarchical cluster display of relative expression levels of the rice HDAC genes in 33 samples representing different organs or tissues at different developmental stages of the Minghui 63 cultivar. 1–5: Calli at different induction stages from cultured embryos. 6: Plumule at 48 h after emergence in the dark. 7: Plumule at 48 h after emergence in the light. 8: Radical at 48 h after emergence in the dark. 9: Radical at 48 h after emergence in the light. 10: 72 h imbibed seed. 11: Embryo and radicle after germination. 12: Seedling leaves and roots at three-leaf stage. 13: Shoots of seedlings with two tillers. 14: Roots of seedlings with two tillers. 15: Stem at day 5 before heading. 16: Stems at heading stage. 17: Leaves from plants at young panicle stage 3. 18: Leaves at young panicle stage 7. 19: Flag leaves at day 5 before heading. 20: Flag leaf at day 14 after heading. 21: Sheaths at young panicle stage 3. 22: Sheaths at young panicle stage 7. 23 : Hulls one day before flowering. 24: Stamens one day before flowering. 25: Young panicle at stage 3. 26: Young panicles at stage 4. 27: Young panicles at stage 5. 28: Panicles at stage 7. 29: Panicles at heading stage. 30: Spikelets, 3 days after pollination. 31: Endosperm, 7 days after pollination. 32: Endosperm, 14 days after pollination. 33: Endosperm, 21 days after pollination. Lower: Expression changes of HDAC genes responding to abiotic stresses including drought, salt and cold in seven-day-old light-grown seedlings. Color bar at the base represents log2 expression values: green, representing low expression; black, medium expression; red, high expression.
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 *Western-blot analysis of enriched histone fractions detected a decrease of H3K9 acetylation in overexpression plants (Fig. 6B). The overexpression plants showed no particular visible or morphological phenotype. However, when treated with paraquat (1,1′-dimethyl-4,4′-bipyridylium), an herbicide that induces oxidative stresses in plants, the overexpression plants showed an enhanced tolerance compared to the wild type, as demonstrated by fewer and smaller lesions observed on the overexpression plants than the wild type.<ref name="ref1" />
-[[File:F2.small.gif|right|thumb|360px|F2.small''<ref name="ref1" />'']]
+[[File:small.gif|right|thumb|360px|small''<ref name="ref1" />'']]
 <br />Expression profiles of OsSRT1. A, Northern hybridization detection of OsSRT1 mRNA in different rice tissues or developmental stages. Actin transcripts were detected as controls. B, Nuclear localization of the OsSRT1-GFP fusion. Top, Onion skin cells transfected with OsSRT1-GFP photographed under a confocal microscope at 488 nm (left) and merged with the transmission image (right). Bottom, GFP alone.<br />
 [[File:F1.medium.gif|right|thumb|360px|F1.medium.''<ref name="ref5" />'']]

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 *Western-blot analysis of enriched histone fractions detected a decrease of H3K9 acetylation in overexpression plants (Fig. 6B). The overexpression plants showed no particular visible or morphological phenotype. However, when treated with paraquat (1,1′-dimethyl-4,4′-bipyridylium), an herbicide that induces oxidative stresses in plants, the overexpression plants showed an enhanced tolerance compared to the wild type, as demonstrated by fewer and smaller lesions observed on the overexpression plants than the wild type.<ref name="ref1" />
 [[File:F1.medium.gif|right|thumb|360px|F1.medium.''<ref name="ref5" />'']]
 <br />Neighbor-joining tree of SIR2-related proteins from eukaryotes. Abbreviations are as follows (in parentheses): Arabidopsis (at), Caenorhabditis elegans (ce), Drosophila melanogaster (dm), Homo sapiens (hs), rice (os), Saccharomyces cerevisiae (sc), Schizosaccharomyces pombe (sp), wheat (ta), and maize (zm). Four subclasses are indicated.<br />

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 *While earlier models suggested sir-2.1 might function by down-regulating insulin signaling, more recent findings show that sir-2.1 binds to DAF-16, activating it directly. Moreover, sir-2.1 does not respond to changes in insulin signaling, but, rather, is activated by stress treatments, such as heat shock and oxidative damage <ref name="ref12" />
-[[File:1-s2.0-S1367593105001079-gr1.gif|right|thumb|360px|1-s2.0-S1367593105001079-gr1.''<ref name="ref21" />'']]
+[[File:1-s2.0-S1367593105001079-gr1.gif|right|thumb|360px|1-s2.0-S1367593105001079-gr1.'']]
 <br />Proposed functions of yeast Sir2 and of mammalian SIRT1. (a) Yeast Sir2 histone deacetylation and silencing function. Acetyl-CoA-dependent histone acetyltransferases acetylate histones leading to transcriptional activation. The NAD+-dependent deacetylase Sir2 deacetylates histones and creates transcriptional silent chromatin. Nicotinamide is a product of the reaction and is a potent inhibitor of Sir2. OAADPr is a novel metabolite generated during deacetylation and may function in linked cellular pathways. An NAD+ salvage pathway depletes nicotinamide and funnels NAD+ to Sir2. (b) General chemical reaction catalyzed by sirtuins. Human SIRT1 is depicted with several reported acetylated protein targets and the pathways affected.<br />

← Older revision		Revision as of 07:47, 10 June 2014
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	*While earlier models suggested sir-2.1 might function by down-regulating insulin signaling, more recent findings show that sir-2.1 binds to DAF-16, activating it directly. Moreover, sir-2.1 does not respond to changes in insulin signaling, but, rather, is activated by stress treatments, such as heat shock and oxidative damage <ref name="ref12" />		*While earlier models suggested sir-2.1 might function by down-regulating insulin signaling, more recent findings show that sir-2.1 binds to DAF-16, activating it directly. Moreover, sir-2.1 does not respond to changes in insulin signaling, but, rather, is activated by stress treatments, such as heat shock and oxidative damage <ref name="ref12" />
		+
		+	[[File:1-s2.0-S1367593105001079-gr1.gif\|right\|thumb\|360px\|1-s2.0-S1367593105001079-gr1.''<ref name="ref21" />'']]
		+	<br />Proposed functions of yeast Sir2 and of mammalian SIRT1. (a) Yeast Sir2 histone deacetylation and silencing function. Acetyl-CoA-dependent histone acetyltransferases acetylate histones leading to transcriptional activation. The NAD+-dependent deacetylase Sir2 deacetylates histones and creates transcriptional silent chromatin. Nicotinamide is a product of the reaction and is a potent inhibitor of Sir2. OAADPr is a novel metabolite generated during deacetylation and may function in linked cellular pathways. An NAD+ salvage pathway depletes nicotinamide and funnels NAD+ to Sir2. (b) General chemical reaction catalyzed by sirtuins. Human SIRT1 is depicted with several reported acetylated protein targets and the pathways affected.<br />

	===Expression===		===Expression===

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 <ref name="ref12">Berdichevsky, A., Viswanathan, M., Horvitz, H.R., Guarente, L.(2006) C. elegans SIR-2.1 interacts with 14–3–3 proteins to activate DAF-16 and extend life span. Cell 125:1165–1177.</ref>
 <ref name="ref13">Grubisha, O., Smith, B.C., Denu, J.M.(2005) Small molecule regulation of Sir2 protein deacetylases. FEBS J. 272:4607–4616.</ref>
 ==Structured Information==
 {{JaponicaGene|

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 <br />Sirtuin deacetylation and ADP-ribosylation reactions. Both deacetylation and ADP-ribosylation occur via cleavage of NAD to release nicotinamide.
-*Mitochondria are central hubs of energy metabolism in plants and animals. In addition to a fine-tuned mitochondria-to-nuclear signaling that regulates transcription of nuclear gene expression.<ref name="ref14" />
+*Mitochondria are central hubs of energy metabolism in plants and animals. In addition to a fine-tuned mitochondria-to-nuclear signaling that regulates transcription of nuclear gene expression,<ref name="ref14" /> posttranslational modifications of proteins are thought to be essential for the regulation of central metabolic pathways and thus determine the plasticity of plant metabolism.<ref name="ref15" /> In mammalian mitochondria, the regulation of metabolic functions by posttranslational Lys acetylation of proteins was recently discovered to be of great importance.<ref name="ref16" /> Lys acetylation can have a strong impact on the biochemical function of proteins as the transfer of the acetyl group to Lys masks the positive charge, which is known to be important in many catalytic centers of enzymes, as well as for protein-protein and protein-DNA interactions. In plants, Lys acetylation was, until recently, mainly thought to occur on histone proteins as regulatory mechanism for transcription and chromatin functions.<ref name="ref17" />However, several central metabolic enzymes of diverse subcellular compartments were recently discovered to be Lys acetylated in Arabidopsis (Arabidopsis thaliana), and in vitro deacetylation tests confirmed that Lys acetylation affects enzyme activities and protein functions.<ref name="ref18" />
 ==Labs working on this gene==