Source:http://linkedlifedata.com/resource/pubmed/id/21241387
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2011-4-18
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pubmed:abstractText |
Major intrinsic proteins (MIPs) transport water and uncharged solutes across membranes in all kingdoms of life. Recently, an uncharacterized MIP subfamily was identified in the genomes of plants and fungi and named X Intrinsic Proteins (XIPs). Here, we describe the genetic features, localization, expression, and functions of a group of Solanaceae XIPs. XIP cDNA and gDNA were cloned from tobacco, potato, tomato, and morning glory. A conserved sequence motif in the first intron of Solanaceae XIPs initiates an RNA-processing mechanism that results in two splice variants (? and ?). When transiently or stably expressed in tobacco plants, yellow fluorescent protein-tagged NtXIP1;1? and NtXIP1;1? were both localized in the plasma membrane. Transgenic tobacco lines expressing NtXIP1;1-promoter-GUS constructs and RT-PCR studies showed that NtXIP1;1 was expressed in all organs. The NtXIP1;1 promoter was mainly active in cell layers facing the environment in all above-ground tissues. Heterologous expression of Solanaceae XIPs in Xenopus laevis oocytes and various Saccharomyces cerevisiae mutants demonstrated that these isoforms facilitate the transport of bulky solutes, such as glycerol, urea, and boric acid. In contrast, permeability for water was undetectable. These data suggest that XIPs function in the transport of uncharged solutes across the cell plasma membrane in specific plant tissues, including at the interface between the environment and external cell layers.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycerol,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Urea,
http://linkedlifedata.com/resource/pubmed/chemical/major intrinsic protein, plant
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1365-313X
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pubmed:author | |
pubmed:copyrightInfo |
© 2011 The Authors. The Plant Journal © 2011 Blackwell Publishing Ltd.
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pubmed:issnType |
Electronic
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
306-17
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pubmed:meshHeading |
pubmed-meshheading:21241387-Animals,
pubmed-meshheading:21241387-Aquaporins,
pubmed-meshheading:21241387-Cell Membrane Permeability,
pubmed-meshheading:21241387-Cloning, Molecular,
pubmed-meshheading:21241387-Flowers,
pubmed-meshheading:21241387-Glycerol,
pubmed-meshheading:21241387-Oocytes,
pubmed-meshheading:21241387-Phylogeny,
pubmed-meshheading:21241387-Plant Proteins,
pubmed-meshheading:21241387-Plant Roots,
pubmed-meshheading:21241387-Saccharomyces cerevisiae,
pubmed-meshheading:21241387-Sequence Analysis, Protein,
pubmed-meshheading:21241387-Solanaceae,
pubmed-meshheading:21241387-Urea,
pubmed-meshheading:21241387-Xenopus
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pubmed:year |
2011
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pubmed:articleTitle |
Solanaceae XIPs are plasma membrane aquaporins that facilitate the transport of many uncharged substrates.
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pubmed:affiliation |
Institut des Sciences de la Vie, Université Catholique de Louvain, Croix du Sud 4-15, B-1348 Louvain-la-Neuve, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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