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BvCOLD1 : A novel aquaporin from sugar beet ( Beta vulgaris L.) involved in boron homeostasis and abiotic stress
Author(s) -
Porcel Rosa,
Bustamante Antonio,
Ros Roc,
Serrano Ramón,
Mulet Salort José M.
Publication year - 2018
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/pce.13416
Subject(s) - aquaporin , sugar beet , biology , bimolecular fluorescence complementation , yeast , abiotic stress , biochemistry , arabidopsis , endoplasmic reticulum , arabidopsis thaliana , botany , gene , microbiology and biotechnology , horticulture , mutant
Beta vulgaris (sugar beet) is one of the most important industrial crops. Screening of a cDNA library for sugar beet genes able to confer cold tolerance upon overexpression in yeast identified a novel aquaporin, which we named BvCOLD1 . The amino acid sequence of BvCOLD1 indicated that an acidic protein (pI 5.18) is similar to tonoplast intrinsic protein aquaporins. RNA expression analysis indicated that BvCOLD1 is expressed in all sugar beet organs. Confocal microscopy of a green fluorescent protein‐tagged version localized BvCOLD1 in the endoplasmic reticulum in yeast and in plant cells. Experiments in yeast showed that BvCOLD1 has an important role in transporting several molecules, among them is boron, one of the most limiting micronutrients for sugar beet cultivation. Transgenic Arabidopsis thaliana plants overexpressing BvCOLD1 showed enhanced tolerance to cold, to different abiotic stresses, and to boron deficiency at different developmental stages. Searches in databases only retrieved BvCOLD1 orthologues in genomes from the Chenopodioideae, a subfamily of the Amaranthaceae family that includes the closely related crop Spinacea oleracea and halotolerant plants such as Salicornia herbacea or Suaeda glauca . Orthologues share a conserved sequence in the carboxy terminus, not present in other aquaporins, which is required for the functionality of the protein.