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1.
Ann Bot ; 105(5): 661-76, 2010 May.
Article in English | MEDLINE | ID: mdl-20299345

ABSTRACT

BACKGROUND: A large proportion of vineyards are located in regions with seasonal drought (e.g. Mediterranean-type climates) where soil and atmospheric water deficits, together with high temperatures, exert large constraints on yield and quality. The increasing demand for vineyard irrigation requires an improvement in the efficiency of water use. Deficit irrigation has emerged as a potential strategy to allow crops to withstand mild water stress with little or no decreases of yield, and potentially a positive impact on fruit quality. Understanding the physiological and molecular bases of grapevine responses to mild to moderate water deficits is fundamental to optimize deficit irrigation management and identify the most suitable varieties to those conditions. SCOPE: How the whole plant acclimatizes to water scarcity and how short- and long-distance chemical and hydraulic signals intervene are reviewed. Chemical compounds synthesized in drying roots are shown to act as long-distance signals inducing leaf stomatal closure and/or restricting leaf growth. This explains why some plants endure soil drying without significant changes in shoot water status. The control of plant water potential by stomatal aperture via feed-forward mechanisms is associated with 'isohydric' behaviour in contrast to 'anysohydric' behaviour in which lower plant water potentials are attained. This review discusses differences in this respect between grapevines varieties and experimental conditions. Mild water deficits also exert direct and/or indirect (via the light environment around grape clusters) effects on berry development and composition; a higher content of skin-based constituents (e.g. tannins and anthocyanins) has generally being reported. Regulation under water deficit of genes and proteins of the various metabolic pathways responsible for berry composition and therefore wine quality are reviewed.


Subject(s)
Adaptation, Physiological/physiology , Plant Transpiration/physiology , Vitis/metabolism , Water/metabolism , Abscisic Acid/metabolism
2.
Planta ; 211(5): 663-72, 2000 Oct.
Article in English | MEDLINE | ID: mdl-11089679

ABSTRACT

1-Aminocyclopropane-1-carboxylate (ACC) synthase (ACS; EC 4.4.1.14) is the key regulatory enzyme of the ethylene biosynthetic pathway and is encoded by a multigene family in Arabidopsis thaliana, tomato, mung bean and other plants. Southern blot analysis revealed the existence of at least five ACS genes in white lupin (Lupinus albus L.) genome. Four complete and one partial sequences representing different ACS genes were cloned from the lupin genomic library. The levels of expression of two of the genes, LA-ACS1 and LA-ACS3, were found to increase after hypocotyl wounding. Apparently, these two genes were up-regulated by exogenous IAA treatment of seedlings. The LA-ACS3 mRNA levels were also elevated in the apical part of hypocotyl, which is reported to contain a high endogenous auxin concentration. This gene may be involved in the auxin- and ethylene-controlled apical hook formation. The expression of the LA-ACS4 gene was found to be almost undetectable. This gene may represent a "silent" twin of LA-ACS5 as these two genes share a considerable level of homology in coding and non-coding regions. The LA-ACS5 mRNA is strongly up-regulated in the embryonic axis of germinating seeds at the time of radicle emergence, and was also found in roots and hypocotyls of lupin seedlings.


Subject(s)
Fabaceae/genetics , Gene Expression Regulation, Plant , Lyases/genetics , Plants, Medicinal , Arabidopsis/enzymology , Arabidopsis/genetics , Base Sequence , Cotyledon/physiology , Fabaceae/enzymology , Fabaceae/growth & development , Gene Expression Regulation, Developmental/drug effects , Gene Expression Regulation, Enzymologic/drug effects , Gene Expression Regulation, Plant/drug effects , Genomic Library , Hypocotyl/physiology , Indoleacetic Acids/pharmacology , Molecular Sequence Data , Multigene Family , Plant Roots/physiology , Promoter Regions, Genetic , Regulatory Sequences, Nucleic Acid , Sequence Alignment
3.
Planta ; 210(4): 543-50, 2000 Mar.
Article in English | MEDLINE | ID: mdl-10787047

ABSTRACT

A cDNA fragment encoding a Lupinus albus. L. class-III chitinase, IF3, was isolated, using a cDNA probe from Cucumis sativus L., by in-situ plaque hybridization from a cDNA library constructed in the Uni-ZAP XR vector, with mRNAs isolated from mature lupin leaves. The cDNA had a coding sequence of 293 amino acids including a 27-residue N-terminal signal peptide. A class-III chitinase gene was detected by Southern analysis in the L. albus genome. Western blotting experiments showed that the IF3 protein was constitutively present during seed development and in all the studied vegetative lupin organs (i.e., roots, hypocotyls and leaves) at two growth stages (7- and 20-d-old plants). Accumulation of both the IF3 mRNA and IF3 protein was triggered by salicylic acid treatment as well as by abiotic (UV-C light and wounding) and biotic stress conditions (Colletotrichum gloeosporioides infection). In necrotic leaves, IF3 chitinase mRNA was present at a higher level than that of another mRNA encoding a pathogenesis-related (PR) protein from L. albus (a PR-10) and that of the rRNAs. We suggest that one role of the IF3 chitinase could be in the defense of the plant against fungal infection, though our results do not exclude other functions for this protein.


Subject(s)
Chitinases/genetics , Rosales/genetics , Amino Acid Sequence , Base Sequence , Blotting, Northern , Blotting, Western , Chitinases/metabolism , Molecular Sequence Data , Plant Proteins , Plant Roots/genetics , Plant Roots/growth & development , Plant Roots/metabolism , Plant Shoots/genetics , Plant Shoots/growth & development , Plant Shoots/metabolism , Rosales/growth & development , Rosales/metabolism , Seeds/genetics , Seeds/growth & development , Seeds/metabolism , Sequence Alignment , Ultraviolet Rays
4.
Plant Physiol ; 110(1): 227-32, 1996 Jan.
Article in English | MEDLINE | ID: mdl-8587984

ABSTRACT

Proteins in the intercellular fluid (IF) of healthy Lupinus albus leaves were characterized. Silver staining of the proteins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed more than 30 polypeptides, with the major ones having a molecular mass lower than 36 kD. After amino-terminal amino acid sequence analysis, one of the major polypeptides, IF4, was shown to have no identity with any of the proteins present in the data bases. Two others, IF1 and IF3, showed identity with previously reported pathogenesis-related proteins, IF1 with an antifungal protein from Hordeum vulgare that belongs to the thaumatin family (PR-5 family), and IF3 with class III chitinase-lysozymes. IF3 was also present in the IF of stem and root and it represents the major polypeptide in the medium of L. albus cell-suspension cultures. The ubiquitous presence of this enzyme in healthy, nonstressed tissues of L. albus cannot be explained.


Subject(s)
Extracellular Space/chemistry , Fabaceae/chemistry , Plant Proteins/chemistry , Plants, Medicinal , Sweetening Agents , Amino Acid Sequence , Cells, Cultured , Chitinases/chemistry , Extracellular Space/drug effects , Extracellular Space/enzymology , Fabaceae/drug effects , Fabaceae/enzymology , Molecular Sequence Data , Salicylates/pharmacology , Salicylic Acid , Sequence Analysis , Sequence Homology, Amino Acid , Tissue Distribution
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