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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
1999-1-14
pubmed:abstractText
By complementation of a salt-sensitive mutant of Saccharomyces cerevisiae, we cloned the SOP1 gene, encoding a 114.5-kDa protein of 1033 amino acids. Cells deleted for SOP1 exhibited sensitivity to sodium stress, but showed no sensitivity to general osmotic stress. Following exposure of sop1Delta cells to NaCl stress, the intracellular Na+ level and the Na+/K+ ratio rose to values significantly higher than in wild type cells. Deletion of SOP2, encoding a protein sharing 54% amino acid identity with Sop1p, produced only slight Na+ sensitivity. Cells carrying a sop1Deltasop2Delta double deletion became, however, hypersensitive to Na+ and exhibited increased sensitivity also to Li+ and K+, suggesting involvement of both SOP1 and SOP2 in cation homeostasis. The predicted amino acid sequences of Sop1p and Sop2p show significant homologies with the cytoskeletal-associated protein encoded by the Drosophila lethal(2)giant larvae tumor suppressor gene. Immunolocalization of Sop1p revealed a cytoplasmic distribution and cell fractionation studies showed that a significant fraction of Sop1p was recovered in a sedimentable fraction of the cytosolic material. Expression of a Drosophila l(2)gl cDNA in the sop1Deltasop2Delta strain partially restored the Na+ tolerance of the cells, indicating a functional relationship between the Sop proteins and the tumor suppressor protein, and a novel function in cell homeostasis for this family of proteins extending from yeast to human.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33610-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9837945-Adaptor Proteins, Signal Transducing, pubmed-meshheading:9837945-Amino Acid Sequence, pubmed-meshheading:9837945-Animals, pubmed-meshheading:9837945-Base Sequence, pubmed-meshheading:9837945-Carrier Proteins, pubmed-meshheading:9837945-Cytoplasm, pubmed-meshheading:9837945-DNA Primers, pubmed-meshheading:9837945-Drosophila, pubmed-meshheading:9837945-Gene Expression Regulation, Fungal, pubmed-meshheading:9837945-Genes, Tumor Suppressor, pubmed-meshheading:9837945-Genetic Complementation Test, pubmed-meshheading:9837945-Homeostasis, pubmed-meshheading:9837945-Humans, pubmed-meshheading:9837945-Molecular Sequence Data, pubmed-meshheading:9837945-Mutation, pubmed-meshheading:9837945-Saccharomyces cerevisiae, pubmed-meshheading:9837945-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9837945-Sequence Homology, Amino Acid, pubmed-meshheading:9837945-Sodium
pubmed:year
1998
pubmed:articleTitle
The Saccharomyces cerevisiae SOP1 and SOP2 genes, which act in cation homeostasis, can be functionally substituted by the Drosophila lethal(2)giant larvae tumor suppressor gene.
pubmed:affiliation
Department of Cell and Molecular Biology, Microbiology, Göteborg University, Box 462, SE 40530 Göteborg, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't