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231223s2011 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2010.09.015
|2 doi
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|a pubmed25n0680.xml
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|a (DE-627)NLM203957148
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|a (NLM)21115356
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Tiwari, Krishnaraj
|e verfasserin
|4 aut
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|a Cloning, expression and functional characterization of the C2 domain from tomato phospholipase Dα
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|c 2011
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 16.08.2011
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|a Date Revised 07.12.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2010 Elsevier Masson SAS. All rights reserved.
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|a C2 domains exist as highly conserved N-terminal or C-terminal calcium- and lipid-binding motifs comprising nearly 130 amino acids, responsible for recruiting proteins to the membrane during signal transduction. In this study, the sequence corresponding to the N-terminal 164 amino acids of a full length cDNA of phospholipase Dα from tomato fruit was cloned in pET28(b) vector and expressed in E. coli as a His-tagged protein. Recombinant C2 domain showed micromolar affinity towards Ca(++) with a maximum of 2 high affinity binding sites. Interaction of C2 domain with synthetic unilamellar vesicles, evaluated by protein- lipid fluorescence resonance energy transfer, showed maximum affinity towards phosphatidic acid, and virtually no binding with phosphatidylcholine. The binding towards phosphoinositides was reduced with increasing degree of phosphorylation. Acid- and chaotropic salt- titrations indicated an electrostatic, rather than a hydrophobic mode of interaction between C2 domain and the phospholipid vesicles. Conformational analyses of the recombinant C2 domain showed a much longer calcium binding loop region, a far less electropositive phosphoinositide-binding region, unique calcium binding pockets with high electro-negativity, and other features that are distinct from the typical C2 domains of phospholipase A2 and Protein kinase C α, signifying the uniqueness of Phospholipase Dα in fruit developmental events
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a DNA, Complementary
|2 NLM
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| 650 |
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|a Phospholipids
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Recombinant Proteins
|2 NLM
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|a Protein Kinase C-alpha
|2 NLM
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| 650 |
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|a EC 2.7.11.13
|2 NLM
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|a Phospholipase D
|2 NLM
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|a EC 3.1.4.4
|2 NLM
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| 650 |
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|a Calcium
|2 NLM
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| 650 |
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|a SY7Q814VUP
|2 NLM
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| 700 |
1 |
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|a Paliyath, Gopinadhan
|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 49(2011), 1 vom: 15. Jan., Seite 18-32
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
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|g volume:49
|g year:2011
|g number:1
|g day:15
|g month:01
|g pages:18-32
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|u http://dx.doi.org/10.1016/j.plaphy.2010.09.015
|3 Volltext
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