Cotton plasma membrane intrinsic protein 2s (PIP2s) selectively interact to regulate their water channel activities and are required for fibre development

Li, Deng-Di; Ruan, Xiang-Mei; Zhang, Jie; Yu, Wu; Wang, Xiulan; Li, Xuebao

doi:10.1111/nph.12309

Cited by 87 publications

(55 citation statements)

References 57 publications

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“…2a), existing as homo-tetramers (Fig. 2b), which was in accord with the classical structures for PIP (Chaumont et al, 2001;Li et al, 2013). Further analysis found that protein EU487188.1, EU487187.1 and AF118383.1 had higher similarity in structure with BnPIP-like protein than AF118381.1 had: AF118381.1 had 7 transmembrane domains and its Cterminal was extracellular (data not shown).…”

Section: Discussionsupporting

confidence: 67%

Expression of Aquaporin BnPIP-like Gene from Rapeseed (Brassica napus) Enhances Salt Resistance in Yeast (Pichia pastoris)

Chai¹,

Li²,

Zhang³

et al. 2016

IJAB

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A new aquaporin (AQP) BnPIP-like gene was isolated and sequenced from rapeseed (Brassica napus L.). It encoded a putative protein with 281 amino acids, sharing 95.3% identity with Arabidopsis plasma membrane intrinsic proteins (PIP, Genbank: NP_195236.1). Prediction of transmembrane structure showed that BnPIP-like gene contained five loops and six transmembrane helices. Online analysis also indicate that BnPIP-like protein existed as homo-tetramers. In order to research its functions in eucaryon, BnPIP-like gene was fused into the pPIC3.5K and then the recombinant vector, as well as the pPIC3.5K, were induced into methylotrophic yeast (Pichia pastoris Strain GS115), respectively. In BMMY media, the BnPIPlike protein was sufficiently expressed after methanol (MeOH) induction for 24 h. The salt stress (300 mM NaCl) treatment was operated after 18 h of normal growth conditions. The OD600 values of BnPIP-like-transgenic P. pastoris and the control were determined every 12 h. The growth curves were obtained and it showed that the growth of both P. pastoris with or without BnPIP-like protein was obviously inhibited. However, the concentrations of BnPIP-like-transgenic P. pastoris was always higher than the control, indicating that the inhibition of growth in BnPIP-like-transgenic P. pastoris was slighter because of the over-expression of BnPIP-like gene. Thus the resistance to salt explained the eukaryotic functions of BnPIPlike protein. Moreover, it provided a theoretical possibility for a more comprehensively industrial utilization of fermenting yeast.

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Section: Discussionsupporting

confidence: 67%

Expression of Aquaporin BnPIP-like Gene from Rapeseed (Brassica napus) Enhances Salt Resistance in Yeast (Pichia pastoris)

Chai¹,

Li²,

Zhang³

et al. 2016

IJAB

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“…TdPIP2;1, as a PIP2 member in wheat, also possesses high water transport activity45. In cotton, expression of GhPIP2;3 also increased a high permeability coefficient of oocytes46. Similarly, tomato SlPIP2;1, SlPIP2;7 and SlPIP2;5 proteins displayed functional water channel activity which increased the osmotic permeability of the X. laevis oocytes 8- to 10-fold (Fig.…”

Section: Discussionmentioning

confidence: 85%

Plasma Membrane Intrinsic Proteins SlPIP2;1, SlPIP2;7 and SlPIP2;5 Conferring Enhanced Drought Stress Tolerance in Tomato

Ren

Wang

et al. 2016

Sci Rep

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The function of aquaporin (AQP) protein in transporting water is crucial for plants to survive in drought stress. With 47 homologues in tomato (Solanum lycopersicum) were reported, but the individual and integrated functions of aquaporins involved in drought response remains unclear. Here, three plasma membrane intrinsic protein genes, SlPIP2;1, SlPIP2;7 and SlPIP2;5, were identified as candidate aquaporins genes because of highly expressed in tomato roots. Assay on expression in Xenopus oocytes demonstrated that SlPIP2s protein displayed water channel activity and facilitated water transport into the cells. With real-time PCR and in situ hybridization analysis, SlPIP2s were considered to be involved in response to drought treatment. To test its function, transgenic Arabidopsis and tomato lines overexpressing SlPIP2;1, SlPIP2;7 or SlPIP2;5 were generated. Compared with wild type, the over-expression of SlPIP2;1, SlPIP2;7 or SlPIP2;5 transgenic Arabidopsis and tomato plants all showed significantly higher hydraulic conductivity levels and survival rates under both normal and drought conditions. Taken together, this study concludes that aquaporins (SlPIP2;1, SlPIP2;7 and SlPIP2;5) contribute substantially to root water uptake in tomato plants through improving plant water content and maintaining osmotic balance.

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“…In cotton, fiber elongation was found to depend on PIP2s and specific PIP2 isoform combinations markedly enhanced the water permeability in Xenopus oocytes (Li et al, 2013). Also, in the halophyte, Thellungiella halophila , ThPIP1 interacted with ThPIP2 and a non-specific lipid-transfer protein 2, suggesting a role of ThPIP1 in the response to the external signals that trigger multiple physiological processes when plants are exposed to salinity (Qiang et al, 2015).…”

Section: Protein–protein Interactionsmentioning

confidence: 99%

Mutual Interactions between Aquaporins and Membrane Components

Martínez-Ballesta

Carvajal

2016

Front. Plant Sci.

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In recent years, a number of studies have been focused on the structural evaluation of protein complexes in order to get mechanistic insights into how proteins communicate at the molecular level within the cell. Specific sites of protein-aquaporin interaction have been evaluated and new forms of regulation of aquaporins described, based on these associations. Heterotetramerizations of aquaporin isoforms are considered as novel regulatory mechanisms for plasma membrane (PIPs) and tonoplast (TIPs) proteins, influencing their intrinsic permeability and trafficking dynamics in the adaptive response to changing environmental conditions. However, protein–protein interaction is an extensive theme that is difficult to tackle and new methodologies are being used to study the physical interactions involved. Bimolecular fluorescence complementation and the identification of cross-linked peptides based on tandem mass spectra, that are complementary to other methodologies such as heterologous expression, co-precipitation assays or confocal fluorescence microscopy, are discussed in this review. The chemical composition and the physical characteristics of the lipid bilayer also influence many aspects of membrane aquaporins, including their functionality. The molecular driving forces stabilizing the positions of the lipids around aquaporins could define their activity, thereby altering the conformational properties. Therefore, an integrative approach to the relevance of the membrane-aquaporin interaction to different processes related to plant cell physiology is provided. Finally, it is described how the interactions between aquaporins and copolymer matrixes or biological compounds offer an opportunity for the functional incorporation of aquaporins into new biotechnological advances.

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Cotton plasma membrane intrinsic protein 2s (PIP2s) selectively interact to regulate their water channel activities and are required for fibre development

Cited by 87 publications

References 57 publications

Expression of Aquaporin BnPIP-like Gene from Rapeseed (Brassica napus) Enhances Salt Resistance in Yeast (Pichia pastoris)

Expression of Aquaporin BnPIP-like Gene from Rapeseed (Brassica napus) Enhances Salt Resistance in Yeast (Pichia pastoris)

Plasma Membrane Intrinsic Proteins SlPIP2;1, SlPIP2;7 and SlPIP2;5 Conferring Enhanced Drought Stress Tolerance in Tomato

Mutual Interactions between Aquaporins and Membrane Components

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