Os05g0519700 - Revision history

192.168.72.52: /* Structured Information */

2015-06-12T07:42:17Z

‎Structured Information

Maple: /* References */

2014-06-10T12:01:30Z

‎References

Maple: /* Evolution */

2014-06-10T11:55:40Z

‎Evolution

Maple: /* References */

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‎References

Maple: /* Expression */

2014-06-10T11:43:16Z

‎Expression

Maple: /* Evolution */

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‎Evolution

Maple: /* Evolution */

2014-06-10T09:36:56Z

‎Evolution

Luckybaby: /* References */

2014-06-10T09:30:46Z

‎References

Luckybaby: /* Expression */

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‎Expression

Luckybaby: /* Expression */

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‎Expression

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 the amino acid sequence of various motifs of plant Hsp100
 members.
 [[Category:Genes]]
 [[Category:Japonica mRNA]]

← Older revision		Revision as of 12:01, 10 June 2014
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	[9] Agarwal M, Katiyar-Agarwal S and Grover A 2002 Plant Hsp100 protein: structure, function and regulation; Plant Sci. 163 397–405		[9] Agarwal M, Katiyar-Agarwal S and Grover A 2002 Plant Hsp100 protein: structure, function and regulation; Plant Sci. 163 397–405
		+
		+	[10] Gaurav Batra, Vineeta Singh Chauhan: Complexity of rice Hsp100 gene family: lessons from rice genome sequence data; J. Biosci.32 611–619.

	==Structured Information==		==Structured Information==

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 it disaggregates and reactivates strongly aggregated proteins. The aggregation reversing activity of ClpB
 requires cooperation with the HSP70/HSP110 chaperone
-machinery.
+machinery<ref name="ref10" />.
 ==Labs working on this gene==

← Older revision		Revision as of 11:45, 10 June 2014
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	[7] Pareek A, Singla SL, Grover A: Immunological evidence for accumulation of two high-molecular-weight (104 and 90 kDa) HSPs in response to different stresses in rice and in response to high temperature stress in diverse plant genera. Plant Molecular Biology 1995, 29(2):293-301.		[7] Pareek A, Singla SL, Grover A: Immunological evidence for accumulation of two high-molecular-weight (104 and 90 kDa) HSPs in response to different stresses in rice and in response to high temperature stress in diverse plant genera. Plant Molecular Biology 1995, 29(2):293-301.
		+
		+	[8] Young T E, Ling J, Geisler-Lee C J, Tanguay R L, Caldwell C and Gallie D R 2001b Developmental and thermal regulation of the maize heat shock protein, HSP101; Plant Physiol. 127 777–791
		+
		+	[9] Agarwal M, Katiyar-Agarwal S and Grover A 2002 Plant Hsp100 protein: structure, function and regulation; Plant Sci. 163 397–405

	==Structured Information==		==Structured Information==

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 Expression characteristics of plant Hsp100 members.Hsp100 transcript/protein expression is induced during heat stress in Arabidopsis, soybean, rice, maize, tobacco and wheat. There are also indications that Hsp100 transcript/protein is induced by desiccation, low temperature and ABA.
-Apart from stress-regulation, Hsp100 transcript and protein are developmentally regulated in plants. In non-stressed maize, Hsp100 is expressed to a high level in the tassel at the pre-meiosis stage, the ear (including silks) and the developing endosperm and embryo.
+Apart from stress-regulation, Hsp100 transcript and protein are developmentally regulated in plants. In non-stressed maize, Hsp100 is expressed to a high level in the tassel at the pre-meiosis stage, the ear (including silks) and the developing endosperm and embryo<ref name="ref8" />.
-Detailed analysis of the amino acid sequence has revealed that Hsp100 members contain several conserved signatures. Schirmer divided Hsp100 into class I (Hsp100 types A–D; containing two nucleotide-binding domains) and class II (Hsp100 types M, N, X, and Y; containing one nucleotide-binding domain) proteins. The molecular weights of the Hsp100 proteins is considered to vary between 75 and 100 kDa because of the size of the non-conserved spacers between the 2 domains and additional sequences at the Cand N-termini. Basically, Hsp100 proteins are composed of five specific domains as follows: (i) amino (N) - terminal domain, (ii) nucleotide – binding domain 1 (NBD1), (iii) middle domain, (iv) NBD2 and (v) carboxyl (C) - terminal domain. The conserved sequences of the five domains include (i) signature sequence I in the N-terminal domain, (ii) Walker A, Walker B1, and Walker B2 sequences in the NBD1, (iii) signature sequence II and signature sequence III in the middle domain, (iv) Walker A and Walker B sequences in NBD2 and (v) signature sequence IV and V in the C-terminal domain. Based on more extensive analysis with larger spectrum of plant species, Agarwal reported further specific alterations in the amino acid sequence of various motifs of plant Hsp100 members.
+Detailed analysis of the amino acid sequence has revealed that Hsp100 members contain several conserved signatures. Schirmer divided Hsp100 into class I (Hsp100 types A–D; containing two nucleotide-binding domains) and class II (Hsp100 types M, N, X, and Y; containing one nucleotide-binding domain) proteins. The molecular weights of the Hsp100 proteins is considered to vary between 75 and 100 kDa because of the size of the non-conserved spacers between the 2 domains and additional sequences at the Cand N-termini. Basically, Hsp100 proteins are composed of five specific domains as follows: (i) amino (N) - terminal domain, (ii) nucleotide – binding domain 1 (NBD1), (iii) middle domain, (iv) NBD2 and (v) carboxyl (C) - terminal domain. The conserved sequences of the five domains include (i) signature sequence I in the N-terminal domain, (ii) Walker A, Walker B1, and Walker B2 sequences in the NBD1, (iii) signature sequence II and signature sequence III in the middle domain, (iv) Walker A and Walker B sequences in NBD2 and (v) signature sequence IV and V in the C-terminal domain. Based on more extensive analysis with larger spectrum of plant species, Agarwal reported further specific alterations in the amino acid sequence of various motifs of plant Hsp100 members<ref name="ref9" />.
 ===Evolution===

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 ===Evolution===
 HSP100 proteins belong to ClpB family. Clp
 ATPases maintain quality of cellular proteins by performing

← Older revision		Revision as of 09:30, 10 June 2014
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	[5] IRGSP: The map-based sequence of the rice genome. Nature 2005, 436(7052):793-800.		[5] IRGSP: The map-based sequence of the rice genome. Nature 2005, 436(7052):793-800.
		+
		+	[6] Singla SL, Grover A: Antibodies raised against yeast HSP 104 cross-react with a heat- and abscisic acid-regulated polypeptide in rice. Plant Molecular Biology 1993, 22(6):1177-1180.
		+
		+	[7] Pareek A, Singla SL, Grover A: Immunological evidence for accumulation of two high-molecular-weight (104 and 90 kDa) HSPs in response to different stresses in rice and in response to high temperature stress in diverse plant genera. Plant Molecular Biology 1995, 29(2):293-301.

	==Structured Information==		==Structured Information==

@@ Line 13: / Line 13: @@
 ===Expression===
-HSP100 is a major heat-regulated protein family in diverse organisms. Across the living systems, common features of HSP100 chaperone action include transient interactions with non-native protein species, in the prevention of aggregation and promotion of correct folding and assembly, or in unfolding for translocation or targeting to proteases. Singla and Grover<ref name="ref6" />
+HSP100 is a major heat-regulated protein family in diverse organisms. Across the living systems, common features of HSP100 chaperone action include transient interactions with non-native protein species, in the prevention of aggregation and promotion of correct folding and assembly, or in unfolding for translocation or targeting to proteases. Singla and Grover showed that homologues of yeast HSP104protein are expressed in heat shocked rice seedlings<ref name="ref6" />. It was subsequently established that apart from heat, rice HSP100 expression is developmentally-controlled as seeds and developing embryos of rice show high constitutive levels of this protein<ref name="ref7" />.
 Expression characteristics of plant Hsp100 members.Hsp100 transcript/protein expression is induced during heat stress in Arabidopsis, soybean, rice, maize, tobacco and wheat. There are also indications that Hsp100 transcript/protein is induced by desiccation, low temperature and ABA.