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231224s2012 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2012.06.006
|2 doi
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|a pubmed24n0730.xml
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|a (DE-627)NLM219229783
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|a (NLM)22771433
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Cha, Joon-Yung
|e verfasserin
|4 aut
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|a Functional characterization of orchardgrass cytosolic Hsp70 (DgHsp70) and the negative regulation by Ca2+/AtCaM2 binding
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|c 2012
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 08.01.2013
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2012 Elsevier Masson SAS. All rights reserved.
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|a When plants are exposed to extreme temperature, stress-inducible proteins are highly induced and involved in subcellular defence mechanisms. Hsp70, one of stress-inducible proteins, functions as an ATP-dependent molecular chaperone in broad organisms to process such as the inhibition of protein denaturation, promotion of protein folding, and renaturation of denatured proteins. In this study, we isolated a heat-inducible orchardgrass Hsp70 (DgHsp70) that is a homolog of cytosolic Hsp70 that possesses a CaM-binding domain. Purified DgHsp70 protein displayed dose-dependent ATPase, holdase, and ATP-dependent foldase activities. To investigate functional roles of DgHsp70 by the association of Arabidopsis calmodulin-2 (AtCaM2), showing heat-sensitive reduction on transcription, we first characterized the binding activity by gel-overlay assay. DgHsp70 binds to AtCaM2 in the presence of Ca(2+) via a conserved CaM-binding domain. Ca(2+)/AtCaM2 binding decreased ATPase activity of DgHsp70, and concomitantly, reduced foldase activity. Based on the protein structure of bovine Hsc70, which is the closest structural homolog of DgHsp70, a CaM-binding domain is located near the ATP-binding site and CaM may span the ATP-binding pocket of Hsp70. Its decreased functional foldase activity may be caused by blocking ATP hydrolysis after Ca(2+)/AtCaM2 binding. It may associate with inhibition of functional activity of DgHsp70 in the absence of stress and/or de novo protein synthesis of DgHsp70 in the presence of thermal stress condition
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Calmodulin
|2 NLM
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|a HSP70 Heat-Shock Proteins
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Adenosine Triphosphate
|2 NLM
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|a 8L70Q75FXE
|2 NLM
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|a Adenosine Triphosphatases
|2 NLM
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| 650 |
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|a EC 3.6.1.-
|2 NLM
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|a Calcium
|2 NLM
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|a SY7Q814VUP
|2 NLM
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| 700 |
1 |
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|a Su'udi, Mukhamad
|e verfasserin
|4 aut
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1 |
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|a Kim, Woe-Yeon
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kim, Deok Ryong
|e verfasserin
|4 aut
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|a Kwak, Youn-Sig
|e verfasserin
|4 aut
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| 700 |
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|a Son, Daeyoung
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 58(2012) vom: 15. Sept., Seite 29-36
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
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|g volume:58
|g year:2012
|g day:15
|g month:09
|g pages:29-36
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|u http://dx.doi.org/10.1016/j.plaphy.2012.06.006
|3 Volltext
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|d 58
|j 2012
|b 15
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|h 29-36
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