Source:http://linkedlifedata.com/resource/pubmed/id/20880842
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
48
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pubmed:dateCreated |
2010-11-24
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pubmed:abstractText |
Disruption of HpURE2 resulted in a low expression of genes encoding nitrate-assimilatory proteins; sensitivity to Li(+), Na(+), and Cd(2+); no induction of ENA1; low levels of the GATA-type transcription factor Gat1; and low intracellular Ca(2+) levels. Gat1 levels were also very low in a ?cnb1 mutant lacking the regulatory subunit of calcineurin. The strain ?ure2 was very sensitive to the calcineurin inhibitor FK506 and displayed several phenotypes reminiscent of ?cnb1. The reporter 4xCDRE-lacZ, containing calcineurin-dependent response elements in its promoter, revealed that calcineurin activation was reduced in Hp?ure2. Expression of ScURE2 in ?ure2 rescued nitrogen catabolite repression and Cd(2+) tolerance but not those phenotypes depending on calcineurin activation, such as salt tolerance and nitrate assimilation gene derepression. Hp?ure2 showed an increased expression of the gene PMR1 encoding the Golgi Ca(2+)-ATPase, whereas that of PMC1 encoding the vacuolar Ca(2+)-ATPase remained unaltered. PMR1 up-regulation was abolished by deletion of the GATA-type transcription factor GAT2 in a Hp?ure2 genetic background, and normal Ca(2+) levels were recovered. Moreover, overexpression of GAT2 or PMR1 yielded strains mimicking the phenotype of the Hp?ure2. This suggests that the low Ca(2+) levels in the Hp?ure2 mutant are due to the high levels of Pmr1 that replenish the Golgi Ca(2+) content, thus acting as a negative signal for Ca(2+) entry into the cell. We conclude that HpUre2 is involved in salt tolerance and also in nitrate assimilation gene derepression via Ca(2+) homeostasis regulation and calcineurin activation, which control the levels of Gat1.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcineurin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Chloride
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1083-351X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
26
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
37551-60
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pubmed:dateRevised |
2011-1-6
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pubmed:meshHeading |
pubmed-meshheading:20880842-Calcineurin,
pubmed-meshheading:20880842-Calcium,
pubmed-meshheading:20880842-Down-Regulation,
pubmed-meshheading:20880842-Fungal Proteins,
pubmed-meshheading:20880842-Gene Expression Regulation, Fungal,
pubmed-meshheading:20880842-Homeostasis,
pubmed-meshheading:20880842-Nitrogen,
pubmed-meshheading:20880842-Pichia,
pubmed-meshheading:20880842-Salt-Tolerance,
pubmed-meshheading:20880842-Sodium Chloride
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pubmed:year |
2010
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pubmed:articleTitle |
Ure2 is involved in nitrogen catabolite repression and salt tolerance via Ca2+ homeostasis and calcineurin activation in the yeast Hansenula polymorpha.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Institute of Biomedical Technologies, Nitrogen Metabolism Group, Universidad de La Laguna, E-38206 La Laguna, Tenerife, Canarias, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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