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rdf:type |
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lifeskim:mentions |
umls-concept:C0017337,
umls-concept:C0043393,
umls-concept:C0084032,
umls-concept:C0162741,
umls-concept:C0442805,
umls-concept:C0679058,
umls-concept:C0765250,
umls-concept:C1547699,
umls-concept:C1752460,
umls-concept:C2260403,
umls-concept:C2700640
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pubmed:issue |
3
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pubmed:dateCreated |
1996-10-9
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pubmed:databankReference |
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pubmed:abstractText |
A cDNA library in a yeast expression vector was prepared from roots of Arabidopsis exposed to salt and was used to select Li(+)-tolerant yeast transformants. The cDNA SAL1 isolated from one of these transformants encodes a polypeptide of 353 amino acid residues. This protein is homologous to the HAL2 and CysQ phosphatases of yeast and Escherichia coli, respectively. Partial cDNA sequences in the data bases indicate that rice produces a phosphatase highly homologous to SAL1 and that a second gene homologous to SAL1 exists in Arabidopsis. The SAL1 protein expressed in E. coli showed 3'(2'),5'-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities. In yeast, SAL1 restored the ability of a hal2/met22 mutant to grow on sulfate as a sole sulfur source, increased the intracellular Li+ tolerance, and modified Na+ and Li+ effluxes. We propose that the product of SAL1 participates in the sulfur assimilation pathway as well as in the phosphoinositide signaling pathway and that changes in the latter may affect Na+ and Li+ fluxes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-1323235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-1479340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-1505513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-16593860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-1660408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-1690719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-1729235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-2138605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-2152105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-2175387,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-2175905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-2525625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-2824473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-3038862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-3607084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-6253491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-6312838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-6390181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-6546423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-7430066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-7732004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-7768897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-7809627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-7972072,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-8029337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-8132612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-8218365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-8393782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8721754-8437581
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Lithium,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotidases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/bisphosphoadenylate 3'-nucleotidase,
http://linkedlifedata.com/resource/pubmed/chemical/inositol-1,4-bisphosphate...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1040-4651
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
529-37
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:8721754-Amino Acid Sequence,
pubmed-meshheading:8721754-Arabidopsis Proteins,
pubmed-meshheading:8721754-Cloning, Molecular,
pubmed-meshheading:8721754-DNA, Complementary,
pubmed-meshheading:8721754-Gene Library,
pubmed-meshheading:8721754-Genes, Plant,
pubmed-meshheading:8721754-Kinetics,
pubmed-meshheading:8721754-Lithium,
pubmed-meshheading:8721754-Magnesium,
pubmed-meshheading:8721754-Molecular Sequence Data,
pubmed-meshheading:8721754-Nucleotidases,
pubmed-meshheading:8721754-Oryza sativa,
pubmed-meshheading:8721754-Phosphoric Monoester Hydrolases,
pubmed-meshheading:8721754-Saccharomyces cerevisiae,
pubmed-meshheading:8721754-Sequence Homology, Amino Acid,
pubmed-meshheading:8721754-Signal Transduction,
pubmed-meshheading:8721754-Sodium,
pubmed-meshheading:8721754-Zea mays
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pubmed:year |
1996
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pubmed:articleTitle |
The SAL1 gene of Arabidopsis, encoding an enzyme with 3'(2'),5'-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast.
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pubmed:affiliation |
Departamento de Biotecnología, Universidad Politécnica de Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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