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231224s2011 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2011.06.002
|2 doi
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|a pubmed25n0699.xml
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|a (DE-627)NLM209649739
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|a (NLM)21723739
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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 |
1 |
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|a Ayadi, Malika
|e verfasserin
|4 aut
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| 245 |
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|a Identification and characterization of two plasma membrane aquaporins in durum wheat (Triticum turgidum L. subsp. durum) and their role in abiotic stress tolerance
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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 15.12.2011
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|a Date Revised 13.12.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2011 Elsevier Masson SAS. All rights reserved.
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|a Plant plasma membrane intrinsic proteins (PIP) cluster in two phylogenetic groups, PIP1 and PIP2 that have different water channel activities when expressed in Xenopus oocytes. PIP2s induce a marked increase of the membrane osmotic water-permeability coefficient (P(f)), whereas PIP1s are generally inactive. Here we report the cloning of two durum wheat (Triticum turgidum L. subsp. durum) cDNAs encoding TdPIP1;1 and TdPIP2;1 belonging to the PIP1 and PIP2 subfamilies, respectively. Contrary to TdPIP1;1, expression of TdPIP2;1 in Xenopus oocytes resulted in an increase in P(f) compared to water-injected oocytes. Co-expression of the non-functional TdPIP1;1 and the functional TdPIP2;1 lead to a significant increase in P(f) compared with oocytes expressing TdPIP2;1 alone. A truncated form of TdPIP2;1, tdpip2;1, missing the first two transmembrane domains, had no water channel activity. Nonetheless, its co-expression with the functional TdPIP2;1 partially inhibits the P(f) and disrupt the activities of plant aquaporins. In contrast to the approach developed in Xenopus oocytes, phenotypic analyses of transgenic tobacco plants expressing TdPIP1;1 or TdPIP2;1 generated a tolerance phenotype towards osmotic and salinity stress. TdPIP1;1 and TdPIP2;1 are differentially regulated in roots and leaves in the salt-tolerant wheat variety when challenged with salt stress and abscisic acid. Confocal microscopy analysis of tobacco roots expressing TdPIP1;1 and TdPIP2;1 fused to the green fluorescent protein showed that the proteins were localized at the plasma membrane
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Aquaporins
|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 Water
|2 NLM
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|a 059QF0KO0R
|2 NLM
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| 700 |
1 |
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|a Cavez, Damien
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Miled, Nabil
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chaumont, François
|e verfasserin
|4 aut
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| 700 |
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|a Masmoudi, Khaled
|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), 9 vom: 01. Sept., Seite 1029-39
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnas
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| 773 |
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|g volume:49
|g year:2011
|g number:9
|g day:01
|g month:09
|g pages:1029-39
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|u http://dx.doi.org/10.1016/j.plaphy.2011.06.002
|3 Volltext
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|d 49
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