Expression and distribution of a vacuolar aquaporin in young and mature leaf tissues of Brassica napus in relation to water fluxes

Frangne, Nathalie; Maeshima, Masayoshi; Schäffner, Anton R.; Mandel, Therese; Martinoia, Enrico; Bonnemain, Jean‐Louis

doi:10.1007/s004250000390

Cited by 52 publications

(38 citation statements)

References 34 publications

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“…TIPs represent a group of aquaporin homologues in plants, which are expressed in vacuolar membranes [28]. Recently, AtTIP2;1 expression in Arabidopsis roots was shown to be upregulated in response to nitrogen starvation [29].…”

Section: Resultsmentioning

confidence: 99%

Aquaporin homologues in plants and mammals transport ammonia

Jahn¹,

Møller²,

et al. 2004

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Section: Resultsmentioning

confidence: 99%

Aquaporin homologues in plants and mammals transport ammonia

Jahn¹,

Møller²,

et al. 2004

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“…Western blotting was carried out using antibodies for TIP [34], PIP [35] and LHCb3 (Agrisera AB, Sweden). Secondary antibodies (anti-rabbit or anti-chicken, coupled to alkaline phosphatase …”

Section: Western Blottingmentioning

confidence: 99%

Quantitative detection of changes in the leaf‐mesophyll tonoplast proteome in dependency of a cadmium exposure of barley (Hordeum vulgare L.) plants

et al. 2009

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Although the vacuole is the most important final store for toxic heavy metals like cadmium (Cd(2+)), our knowledge on how they are transported into the vacuole is still insufficient. It has been suggested that Cd(2+) can be transported as phytochelatin-Cd(2+) by an unknown ABC transporter or in exchange with protons by cation/proton exchanger (CAX) transporters. To unravel the contribution of vacuolar transporters to Cd(2+) detoxification, a quantitative proteomics approach was performed. Highly purified vacuoles were isolated from barley plants grown under minus, low (20 microM), and high (200 microM) Cd(2+ )conditions and protein levels of the obtained tonoplast samples were analyzed using isobaric tag for relative and absolute quantitation (iTRAQ). Although 56 vacuolar transporter proteins were identified, only a few were differentially expressed. Under low-Cd(2+) conditions, an inorganic pyrophosphatase and a gamma-tonoplast intrinsic protein (gamma-TIP) were up-regulated, indicating changes in energization and water fluxes. In addition, the protein ratio of a CAX1a and a natural resistance-associated macrophage protein (NRAMP), responsible for vacuolar Fe(2+) export was increased. CAX1a might play a role in vacuolar Cd(2+) transport. An increase in NRAMP activity leads to a higher cytosolic Fe(2+) concentration, which may prevent the exchange of Fe(2+) by toxic Cd(2+). Additionally, an ABC transporter homolog to AtMRP3 showed up-regulation. Under high Cd(2+) conditions, the plant response was more specific. Only a protein homologous to AtMRP3 that showed already a response under low Cd(2+) conditions, was up-regulated. Interestingly, AtMRP3 is able to partially rescue a Cd(2+)-sensitive yeast mutant. The identified transporters are good candidates for further investigation of their roles in Cd(2+) detoxification. AbstractAlthough the vacuole is the most important final store for toxic heavy metals like cadmium (Cd 2+ ), our knowledge on how they are transported into the vacuole is still scarce. It has been suggested that Cd 2+ can be transported either as phytochelatin-Cd 2+ by an unknown ABC transporter or in exchange with protons by CAX transporters. To unravel the contribution of vacuolar transporters to Cd 2+ detoxification, a quantitative proteomics approach was performed.Highly purified vacuoles were isolated from barley plants grown under minus, low (20 µM), and high (200 µM) Cd 2+ conditions and protein levels of the obtained tonoplast samples were analyzed using iTRAQ TM . Although, 56 vacuolar transporter proteins were identified, however only a few were differentially expressed. Under low-Cd 2+ conditions an inorganic pyrophosphatase and a γ-tonoplast intrinsic protein (γ-TIP) were upregulated, indicating changes in energization and water fluxes. In addition, the protein ratio of a calcium/proton exchanger (CAX1a) and an NRAMP, responsible for vacuolar Fe 2+ export were increased. CAX1a might play a role in vacuolar Cd 2+ transport. An increase in NRAMP activity leads to a higher cytosol...

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“…A study of the distribution of PIP1 and TIP1 homologous proteins in leaves of Brassica napus showed that both types of protein were present in phloem elements of the minor veins but at a much lower level than in parenchyma cells of mesophyll and vascular bundles (Frangne et al, 2001). In phloem sap of barley transcripts of the PIP1 member emip have been detected (Doering-Saad et al, 2002).…”

Section: Aquaporins and The Water Relations Of Developing Seedsmentioning

confidence: 99%

Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies

et al. 2003

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Water and nutrients required by developing seeds are mainly supplied by the phloem and have to be released from a maternal parenchyma tissue before being utilized by the filial tissues of embryo and endosperm. To identify aquaporins that could be involved in this process four full-length cDNAs were cloned and sequenced from a cDNA library of developing seed coats of pea (Pisum sativum L.). The cDNA of PsPIP1-1 appeared to be identical to that of clone 7a/TRG-31, a turgor-responsive gene cloned previously from pea roots. PsPIP1-1, PsPIP2-1, and PsTIP1-1, or their possible close homologues, were also expressed in cotyledons of developing and germinating seeds, and in roots and shoots of seedlings, but transcripts of PsNIP-1 were only detected in the seed coat. In mature dry seeds, high hybridization signals were observed with the probe for PsPIP1-1, but transcripts of PsPIP2-1, PsTIP1-1, and PsNIP-1 were not detected. Functional characterization after heterologous expression in Xenopus oocytes showed that PsPIP2-1 and PsTIP1-1 are aquaporins whereas PsNIP-1 is an aquaglyceroporin. PsNIP-1, like several other NIPs, contains a tryptophan residue corresponding with Trp-48 in GlpF (the glycerol facilitator of Escherichia coli) that borders the selectivity filter in the permeation channel. It is suggested that PsPIP1-1 and/or its possible close homologues could play a role in water absorption during seed imbibition, and that PsPIP2-1, possibly together with PsPIP1-1, could be involved in the release of phloem water from the seed coat symplast, which is intimately connected with the release of nutrients for the embryo.Abbreviations: MIPs, major intrinsic proteins; NIPs, nodulin 26-like intrinsic proteins; PIPs, plasma membrane intrinsic proteins; SIPs, small, basic intrinsic proteins; TIPs, tonoplast intrinsic proteins

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Expression and distribution of a vacuolar aquaporin in young and mature leaf tissues of Brassica napus in relation to water fluxes

Cited by 52 publications

References 34 publications

Aquaporin homologues in plants and mammals transport ammonia

Aquaporin homologues in plants and mammals transport ammonia

Quantitative detection of changes in the leaf‐mesophyll tonoplast proteome in dependency of a cadmium exposure of barley (Hordeum vulgare L.) plants

Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies

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