Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-5-19
pubmed:abstractText
Genes encoding homologues of known amino-acid permeases were deleted in a strain also deficient in the general amino-acid permease. The uptake capacity of the mutants was investigated for several L-alpha-amino acids. Deletion of a gene denoted DIP5 results in the loss of L-aspartate and L-glutamate uptake. The dip5 mutation caused a several hundred-fold reduction of uptake of the two amino acids, both in cells grown on proline as a nitrogen source and in cells grown on ammonium. DIP5-dependent uptake of L-aspartate and L-glutamate was somewhat lower in ammonium-grown cells than in proline-grown cells. Transcriptional regulation is at least partially responsible for this difference, as shown by assaying the DIP5 promoter fused to lacZ. This suggests that the promoter is subject to nitrogen catabolite repression. Transport of a few other amino acids was moderately affected by dip5 but was not competed by L-aspartate in the DIP5 parental strain; transport of these amino acids is therefore unlikely to be mediated by Dip5p. Our results suggest that DIP5 encodes an amino-acid permease with a high transport capacity and a high affinity for L-glutamate and L-aspartate, with a Kt of about 50 microM for both.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0172-8083
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Dip5p mediates high-affinity and high-capacity transport of L-glutamate and L-aspartate in Saccharomyces cerevisiae.
pubmed:affiliation
Department of Yeast Genetics, Carlsberg Laboratory, DK-2500 Copenhagen Valby, Denmark. breg@crc.dk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't