Source:http://linkedlifedata.com/resource/pubmed/id/16550352
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2006-5-17
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pubmed:abstractText |
Schizosaccharomyces pombe isp6(+) gene encodes a vacuolar serine protease, which is specifically induced during nitrogen starvation. An isp6-disruption mutant, isp6Delta, grew normally under normal conditions but was defective in large-scale protein degradation during nitrogen starvation, a hallmark of autophagy. Vacuoles are the organelles for such drastic protein degradation but those of isp6Delta were apparently aberrant. isp6Delta was infertile under nitrogen source-free conditions with poor expression of ste11(+), a gene critical for sexual development. A protein kinase A-disruption mutant, pka1Delta, is prone to sexual development because expression of ste11(+) is derepressed. However, isp6Deltapka1Delta still showed defects in ste11(+) expression and sexual development under nitrogen source-free conditions. isp6Delta and isp6Deltapka1Delta were able to initiate sexual development to produce spores when only a small amount of a nitrogen source was present. Pat1 protein kinase negatively controls meiosis, and a temperature-sensitive mutant of pat1, pat1-114, initiates meiosis irrespective of ploidy at the restrictive temperature. However, isp6Deltapat1-114 did not start meiosis under nitrogen source-free conditions even at the restrictive temperature. These observations suggest that isp6(+) contributes to sexual development by providing a nitrogen source through autophagy.
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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/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/isp6 protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/ste11 protein, S pombe
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0172-8083
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
403-13
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16550352-Autophagy,
pubmed-meshheading:16550352-Epistasis, Genetic,
pubmed-meshheading:16550352-Gene Expression Regulation, Fungal,
pubmed-meshheading:16550352-Meiosis,
pubmed-meshheading:16550352-Membrane Proteins,
pubmed-meshheading:16550352-Nitrogen,
pubmed-meshheading:16550352-Schizosaccharomyces,
pubmed-meshheading:16550352-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:16550352-Serine Endopeptidases,
pubmed-meshheading:16550352-Signal Transduction,
pubmed-meshheading:16550352-Transcription Factors
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pubmed:year |
2006
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pubmed:articleTitle |
A starvation-specific serine protease gene, isp6+, is involved in both autophagy and sexual development in Schizosaccharomyces pombe.
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pubmed:affiliation |
Department of Chemistry, Faculty of Science, Shizuoka University, 836 Oya, 422-8539, Shizuoka, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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