Linked Life Data

9177057

Source:http://linkedlifedata.com/resource/pubmed/id/9177057

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-8-26
pubmed:abstractText
Potato (Solanum tuberosum cv. Désirée) plants expressing yeast invertase directed either to the apoplast, vacuole or cytosol were biochemically and physiologically characterised. All lines of transgenic plants showed similarities to plants growing under water stress. Transformants were retarded in growth, and accumulated hexoses and amino acids, especially proline, to levels up to 40-fold higher than those of the wild types. In all transformants rates of CO2 assimilation and leaf conductance were reduced. From the unchanged intercellular partial pressure of CO2 and apoplastic cis-abscisic acid (ABA) content of transformed leaves it was concluded that the reduced rate of CO2 assimilation was not caused by a limitation in the availability of CO2 for the ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco). In the transformants the amount of Rubisco protein was not reduced, but both activation state and carboxylation efficiency of photosynthesis were lowered. In vacuolar and cytosolic transformants this inhibition of Rubisco might be caused by a changed ratio of organic bound and inorganic phosphate, as indicated by a doubling of phosphorylated intermediates. But in apoplastic transformants the pattern of phosphorylated intermediates resembled that of leaves of water-stressed potato plants, although the cause of inhibition of photosynthesis was not identical. Whereas in water-stressed plants increased contents of the phytohormone ABA are supposed to mediate the adaptation to water stress, no contribution of ABA to reduction of photosynthesis could be detected in invertase transformants.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0032-0935
pubmed:author
pubmed:issnType
Print
pubmed:volume
202
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
126-36
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9177057-Abscisic Acid, pubmed-meshheading:9177057-Carbon Dioxide, pubmed-meshheading:9177057-Chlorophyll, pubmed-meshheading:9177057-Cytosol, pubmed-meshheading:9177057-Fungal Proteins, pubmed-meshheading:9177057-Gene Expression, pubmed-meshheading:9177057-Glycoside Hydrolases, pubmed-meshheading:9177057-Hexoses, pubmed-meshheading:9177057-Phenotype, pubmed-meshheading:9177057-Phosphorylation, pubmed-meshheading:9177057-Photosynthesis, pubmed-meshheading:9177057-Plant Leaves, pubmed-meshheading:9177057-Plants, Genetically Modified, pubmed-meshheading:9177057-Proline, pubmed-meshheading:9177057-Recombinant Fusion Proteins, pubmed-meshheading:9177057-Ribulose-Bisphosphate Carboxylase, pubmed-meshheading:9177057-Solanum tuberosum, pubmed-meshheading:9177057-Vacuoles, pubmed-meshheading:9177057-Water, pubmed-meshheading:9177057-Water-Electrolyte Balance, pubmed-meshheading:9177057-Yeasts, pubmed-meshheading:9177057-beta-Fructofuranosidase
pubmed:year
1997
pubmed:articleTitle
Solute accumulation and decreased photosynthesis in leaves of potato plants expressing yeast-derived invertase either in the apoplast, vacuole or cytosol.
pubmed:affiliation
Institut für Biochemie der Pflanze, Göttingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't