Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1992-5-12
pubmed:abstractText
Little is known about the degradation of the most abundant protein in nature, ribulose-bisphosphate carboxylase (RuBP carboxylase, EC 4.1.1.39), probably reflecting the fact that no stress situation has been identified capable of causing extensive RuBP carboxylase degradation without causing the death of the plant. We have subjected plants of Lemna minor L. to a variety of stress situations, nutritive deficiencies in particular, and have found a single condition--sulfur starvation--that caused almost complete degradation of RuBP carboxylase without causing plant death. Moreover, the enzyme was preferentially degraded under these conditions. However, when the plants were deprived of calcium, no RuBP carboxylase degradation was observed. Instead, the enzyme was oxidized and polymerized into high molecular mass aggregates. On the other hand, RuBP carboxylase shows an extreme stability when Lemna is deprived of some macronutrients (e.g. nitrogen, phosphorus, potassium, and magnesium) probably reflecting that this plant had to evolve in a way to cope with frequent shortages of such elements. The implications of these data for the role of RuBP carboxylase as a leaf storage protein are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7253-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Sulfur starvation in Lemna leads to degradation of ribulose-bisphosphate carboxylase without plant death.
pubmed:affiliation
Departamento de Botânica e Engenharia Biológica, Instituto Superior de Agronomia, Lisboa, Portugal.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't