Os11g0703900 - Revision history

Luckybaby: /* References */

2014-06-09T15:54:52Z

‎References

Luckybaby: /* Expression */

2014-06-09T15:53:45Z

‎Expression

Luckybaby: /* Function */

2014-06-09T15:53:21Z

‎Function

Luckybaby: /* Function */

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‎Function

Maple: /* Expression */

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‎Expression

Maple: /* Expression */

2014-06-09T15:14:33Z

‎Expression

Maple: /* Function */

2014-06-09T15:12:59Z

‎Function

Qianying: /* Expression */

2014-06-09T15:07:34Z

‎Expression

Qianying: /* References */

2014-06-09T15:04:34Z

‎References

Qianying: /* Expression */

2014-06-09T15:01:15Z

‎Expression

← Older revision		Revision as of 15:54, 9 June 2014
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	<ref name="ref18">Frank Van Breusegem, Rudy Dekeyser, Ana Beatriz Garcia,et al.Heat-inducible rice hsp82 and hsp70 are not always co-regulated[J].Planta, 1994, 193(1): 57-66.</ref>		<ref name="ref18">Frank Van Breusegem, Rudy Dekeyser, Ana Beatriz Garcia,et al.Heat-inducible rice hsp82 and hsp70 are not always co-regulated[J].Planta, 1994, 193(1): 57-66.</ref>
		+
		+	<ref name="ref19">Kuzmin, E.V., Karpova, O.V., Elthon, T.E. and Newton, K.J. Mitochondrial respiratory deficiencies signal up-regulation of genes for heat shock proteins. J. Biol. Chem. 2004. 279, 20672–20677.</ref>
		+
	<references>		<references>

← Older revision		Revision as of 15:53, 9 June 2014
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	*The stress induced expression profile of Hsp70 superfamily genes showed diverse response.		*The stress induced expression profile of Hsp70 superfamily genes showed diverse response.
		+
		+	*During heat stress the expression of hsp70 correlates well with increases in internal ion concentrations, and can also be induced by excess salt or ethanol at normal growth temperatures.

	===Evolution===		===Evolution===

← Older revision		Revision as of 15:53, 9 June 2014
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	*In animal cells, the loss of mtHsp70 protein content in the marginal zone may lead to decreased functional mitochondria, whereas mtHsp70 over-expression preserves mitochondrial function, lessens oxidative stress and subsequent apoptosis<ref name="ref19" />.		*In animal cells, the loss of mtHsp70 protein content in the marginal zone may lead to decreased functional mitochondria, whereas mtHsp70 over-expression preserves mitochondrial function, lessens oxidative stress and subsequent apoptosis<ref name="ref19" />.
		+
		+	*overexpression of mtHsp70 effectively reduced the percentage of dead cells (39.8% after 6 h recovery) compared with VC (63.2% after 6 h recovery).

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

← Older revision		Revision as of 15:52, 9 June 2014
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	*Heat stress results in misfolding and aggregation of cellular proteins. Heat shock proteins (Hsp) enable the cells to maintain proper folding of proteins, both in unstressed as well as stressed conditions. Hsp70 genes encode for a group of highly conserved chaperone proteins across the living systems encompassing bacteria, plants, and animals. In the cellular chaperone network, Hsp70 family proteins interconnect other chaperones and play a dominant role in various cell processes.		*Heat stress results in misfolding and aggregation of cellular proteins. Heat shock proteins (Hsp) enable the cells to maintain proper folding of proteins, both in unstressed as well as stressed conditions. Hsp70 genes encode for a group of highly conserved chaperone proteins across the living systems encompassing bacteria, plants, and animals. In the cellular chaperone network, Hsp70 family proteins interconnect other chaperones and play a dominant role in various cell processes.
		+
		+	*In animal cells, Hsp70s play an anti-apoptotic role via two pathways. In one, Hsp70 binds directly to Apaf-1 and inhibits the formation of apoptosomes. In the other, Hsp70 interacts with members of the Bcl-2 family, and inhibits the release of cytochrome c, endonucleases, and apoptosis-inducing factor from mitochondria to the cytosol<ref name="ref10" />.
		+
		+	*In animal cells, the loss of mtHsp70 protein content in the marginal zone may lead to decreased functional mitochondria, whereas mtHsp70 over-expression preserves mitochondrial function, lessens oxidative stress and subsequent apoptosis<ref name="ref19" />.

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

@@ Line 30: / Line 30: @@
 *Overexpression of Hsp70 will decrease the concentration of Ca2+ intracellular<ref name="ref13" />, which usually works as a second messenger to stimulate the activity of protein kinases in downstream when the organism faces an environmental stress<ref name="ref14" />.
-*Hsp70 are ATP-dependent chaperones having a conserved ~44-kD N-terminal ATPase domain (also called nucleotide binding domain; NBD), a ~18-kD substrate binding domain (SBD) and a ~10-kD variable C-terminal “lid.”<ref name="ref4" />.
+*Hsp70 are ATP-dependent chaperones having a conserved ~44-kD N-terminal ATPase domain (also called nucleotide binding domain; NBD), a ~18-kD substrate binding domain (SBD) and a ~10-kD variable C-terminal “lid.”.
-*Hsp70 proteins require two cochaperones in the form of J-domain proteins and nucleotide
+*Hsp70 proteins require two cochaperones in the form of J-domain proteins and nucleotide exchange factors (NEFs) for their functions. Binding of J-domain proteins stimulates ATP hydrolysis that facilitates trapping of exposed hydrophobic region of substrates and closed conformation of SBD. NEFs participate in ATP–ADP exchange by catalyzing the release of ADP from Hsp70, leading to conversion of open conformation Hsp70 and substrate release<ref name="ref4" />.
 *The stress induced expression profile of Hsp70 superfamily genes showed diverse response.

← Older revision		Revision as of 15:14, 9 June 2014
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	*Overexpression of Hsp70 will decrease the concentration of Ca2+ intracellular<ref name="ref13" />, which usually works as a second messenger to stimulate the activity of protein kinases in downstream when the organism faces an environmental stress<ref name="ref14" />.		*Overexpression of Hsp70 will decrease the concentration of Ca2+ intracellular<ref name="ref13" />, which usually works as a second messenger to stimulate the activity of protein kinases in downstream when the organism faces an environmental stress<ref name="ref14" />.
		+
		+	*Hsp70 are ATP-dependent chaperones having a conserved ~44-kD N-terminal ATPase domain (also called nucleotide binding domain; NBD), a ~18-kD substrate binding domain (SBD) and a ~10-kD variable C-terminal “lid.”<ref name="ref4" />.
		+
		+	*Hsp70 proteins require two cochaperones in the form of J-domain proteins and nucleotide
		+	exchange factors (NEFs) for their functions. Binding of J-domain proteins stimulates ATP hydrolysis that facilitates trapping of exposed hydrophobic region of substrates and closed conformation of SBD. NEFs participate in ATP–ADP exchange by catalyzing the release of ADP from Hsp70, leading to conversion of open conformation Hsp70 and substrate release.
		+
		+	*The stress induced expression profile of Hsp70 superfamily genes showed diverse response.

	===Evolution===		===Evolution===

← Older revision		Revision as of 15:12, 9 June 2014
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	*It is noted that Hsp70 may function as a negative feedback regulator of HSF activity<ref name="ref6" /><ref name="ref7" />.In this process, Hsp70 binds to denatured proteins and releases HSF leading to its activation during heat stress<ref name="ref6" />.		*It is noted that Hsp70 may function as a negative feedback regulator of HSF activity<ref name="ref6" /><ref name="ref7" />.In this process, Hsp70 binds to denatured proteins and releases HSF leading to its activation during heat stress<ref name="ref6" />.
		+
		+	*Heat stress results in misfolding and aggregation of cellular proteins. Heat shock proteins (Hsp) enable the cells to maintain proper folding of proteins, both in unstressed as well as stressed conditions. Hsp70 genes encode for a group of highly conserved chaperone proteins across the living systems encompassing bacteria, plants, and animals. In the cellular chaperone network, Hsp70 family proteins interconnect other chaperones and play a dominant role in various cell processes.

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

@@ Line 24: / Line 24: @@
 [[File:Fig.2. Over-expression of mtHSP70 suppressed H2O2-induced PCD in rice protoplasts.jpg|right|thumb|360px|Fig.2. Over-expression of mtHSP70 suppressed H2O2-induced PCD in rice protoplasts..<ref name="ref11" />'']]
-*Hsp70 regulates the expression of stress response genes, such as the regulation of the heat shock protein transcription factor (heat-shock factor, HSF)<ref name="ref5" /><ref name="ref12" />.
+*Hsp70 regulates the expression of stress response genes, such as the regulation of the heat shock protein transcription factor (heat-shock factor, HSF)<ref name="ref8" /><ref name="ref12" />.
 *Overexpression of Hsp70 will decrease the concentration of Ca2+ intracellular<ref name="ref13" />, which usually works as a second messenger to stimulate the activity of protein kinases in downstream when the organism faces an environmental stress<ref name="ref14" />.

@@ Line 66: / Line 66: @@
 <ref name="ref7">Kim B H, Schöffl F. Interaction between Arabidopsis heat shock transcription factor 1 and 70 kDa heat shock proteins[J]. Journal of experimental botany, 2002, 53(367): 371-375.</ref>
-<ref name="ref8">Muench D G, Wu Y, Zhang Y, et al. Molecular cloning, expression and subcellular localization of a BiP homolog from rice endosperm tissue[J]. Plant and cell physiology, 1997, 38(4): 404-412.</ref>
+<ref name="ref8">Sarkar N K, Kundnani P, Grover A. Functional analysis of Hsp70 superfamily proteins of rice (Oryza sativa)[J]. Cell Stress and Chaperones, 2013, 18(4): 427-437.</ref>
-<ref name="ref9">Snowden C J, Leborgne‐Castel N, Wootton L J, et al. In vivo analysis of the lumenal binding protein (BiP) reveals multiple functions of its ATPase domain[J]. The Plant Journal, 2007, 52(6): 987-1000. </ref>
+<ref name="ref9">Muench D G, Wu Y, Zhang Y, et al. Molecular cloning, expression and subcellular localization of a BiP homolog from rice endosperm tissue[J]. Plant and cell physiology, 1997, 38(4): 404-412.</ref>
-<ref name="ref10">Qi Y, Wang H, Zou Y, et al. Over-expression of mitochondrial heat shock protein 70 suppresses programmed cell death in rice[J]. FEBS letters, 2011, 585(1): 231-239.</ref>
+<ref name="ref10">Snowden C J, Leborgne‐Castel N, Wootton L J, et al. In vivo analysis of the lumenal binding protein (BiP) reveals multiple functions of its ATPase domain[J]. The Plant Journal, 2007, 52(6): 987-1000. </ref>
-<ref name="ref11"> Kim BH, Schöffl F. Interaction between Arabidopsis heat shock transcription factor 1 and 70 kDa heat shock proteins. Journal of Experimental Botany 2002, 53(367):371-375.</ref>
+<ref name="ref11">Qi Y, Wang H, Zou Y, et al. Over-expression of mitochondrial heat shock protein 70 suppresses programmed cell death in rice[J]. FEBS letters, 2011, 585(1): 231-239.</ref>
-<ref name="ref12">  Kiang JG, Ding XZ, McClain DE. Overexpression of HSP-70 attenuates increases in [Ca2+]I and protects human epidermoid A-431 cells after chemical hypoxia. Toxicology and Applied Pharmacology 1998, 149(2):185-194.</ref>
+<ref name="ref12"> Kim BH, Schöffl F. Interaction between Arabidopsis heat shock transcription factor 1 and 70 kDa heat shock proteins. Journal of Experimental Botany 2002, 53(367):371-375.</ref>
-<ref name="ref13">Knight H: Calcium signaling during abiotic stress in plants. International Review of Cytology 2000, 195:269-324.</ref>
+<ref name="ref13">  Kiang JG, Ding XZ, McClain DE. Overexpression of HSP-70 attenuates increases in [Ca2+]I and protects human epidermoid A-431 cells after chemical hypoxia. Toxicology and Applied Pharmacology 1998, 149(2):185-194.</ref>
-<ref name="ref14">Walsh P, Bursać D, Law Y C, et al. The J‐protein family: modulating protein assembly, disassembly and translocation[J]. EMBO reports, 2004, 5(6): 567-571.</ref>
+<ref name="ref14">Knight H: Calcium signaling during abiotic stress in plants. International Review of Cytology 2000, 195:269-324.</ref>
-<ref name="ref15"> Lin B L, Wang J S, Liu H C, et al. Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana[J]. Cell stress & chaperones, 2001, 6(3): 201.</ref>
+<ref name="ref15">Walsh P, Bursać D, Law Y C, et al. The J‐protein family: modulating protein assembly, disassembly and translocation[J]. EMBO reports, 2004, 5(6): 567-571.</ref>
-<ref name="ref16"> Guy C L, Li Q B. The organization and evolution of the spinach stress 70 molecular chaperone gene family[J]. The Plant Cell Online, 1998, 10(4): 539-556.</ref>
+<ref name="ref16"> Lin B L, Wang J S, Liu H C, et al. Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana[J]. Cell stress & chaperones, 2001, 6(3): 201.</ref>
-<ref name="ref17">Frank Van Breusegem, Rudy Dekeyser, Ana Beatriz Garcia,et al.Heat-inducible rice hsp82 and hsp70 are not always co-regulated[J].Planta, 1994, 193(1): 57-66.</ref>
+<ref name="ref17"> Guy C L, Li Q B. The organization and evolution of the spinach stress 70 molecular chaperone gene family[J]. The Plant Cell Online, 1998, 10(4): 539-556.</ref>
 <references>

@@ Line 16: / Line 16: @@
 *Rice Hsp70 superfamily genes are represented by 24 Hsp70 family and 8 Hsp110 family members<ref name="ref4" />.
-*In rice, ER Hsp70 (BiP) is found to associate with nascent polypeptides that emerge into the ER lumen during prolamin translocation and facilitate peptide folding and assembly<ref name="ref4" />. Over-expression of BiP relieves "ER stress"<ref name="ref10" />.
+*In rice, ER Hsp70 (BiP) is found to associate with nascent polypeptides that emerge into the ER lumen during prolamin translocation and facilitate peptide folding and assembly<ref name="ref9" />. Over-expression of BiP relieves "ER stress"<ref name="ref10" />.
 *Rice mitochondrial Hsp70 has been proposed as suppressor of heat and H2O2-induced programmed cell death<ref name="ref11" />.