Linked Life Data

8647819

Source:http://linkedlifedata.com/resource/pubmed/id/8647819

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1996-7-22
pubmed:databankReference
pubmed:abstractText
An Arabidopsis thaliana ATP sulfurylase cDNA (ASA1), encoding a putative chloroplastic isoform, has been cloned by functional complementation of a Saccharomyces cerevisiae (met3) ATP sulfurylase mutant which also has a poor sulfate transport capacity. Homologous complementation of the yeast mutant with the ATP sulfurylase gene restores both ATP sulfurylase function and sulfate transport. Heterologous complementation restores only ATP sulfurylase function as demonstrated by low [35S]sulfate influx measurements and selenate resistance. A structural relationship between ATP sulfurylase and sulfate membrane transporters in yeast is proposed. The sequence of ASA1 is homologous to deduced plant and animal ATP sulfurylase sequences. Analyses indicate a potential tyrosine phosphorylation site which is unique to higher eukaryote sequences. ASA1 is specified by a single copy gene that is part of a multigene family in A. thaliana. At least two ASA1 copies are found in Brassica napus plants. ASA1 transcripts were found in all organs examined, with the highest transcript abundance and ATP sulfurylase activity in leaves or cotyledons. Absence of sulfate from culture media transiently increased B. napus transcript abundance, indicating that initially, the response to sulfate deprivation is transcriptionally regulated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12227-33
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Cloning of a cDNA encoded by a member of the Arabidopsis thaliana ATP sulfurylase multigene family. Expression studies in yeast and in relation to plant sulfur nutrition.
pubmed:affiliation
Ecole Nationale Supe?ieure Agronomique de Montpellier, Institut National de la Recherche Agronomique, CNRS (ura 573), France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't