Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1998-12-24
pubmed:abstractText
Cell type control of meiotic gene regulation in the budding yeast Saccharomyces cerevisiae is mediated by a cascade of transcriptional repressors, a1-alpha2 and Rme1. Here, we investigate the analogous regulatory pathway in the fission yeast Schizosaccharomyces pombe by analyzing the promoter of mei3, the single gene whose expression is sufficient to trigger meiosis. The mei3 promoter does not appear to contain a negative regulatory element that represses transcription in haploid cells. Instead, correct regulation of mei3 transcription depends on a complex promoter that contains at least five positive elements upstream of the TATA sequence. These elements synergistically activate mei3 transcription, thereby constituting an on-off switch for the meiosis pathway. Element C is a large region containing multiple sequences that resemble binding sites for Mc, an HMG domain protein encoded by the mating-type locus. The function of element C is extremely sensitive to spacing changes but not to linker-scanning mutations, suggesting the possibility that Mc functions as an architectural transcription factor. Altered-specificity experiments indicate that element D interacts with Pm, a homeodomain protein encoded by the mating-type locus. This indicates that Pm functions as a direct activator of the meiosis pathway, whereas the homologous mating-type protein in S. cerevisiae (alpha2) functions as a repressor. Thus, despite the strong similarities between the mating-type loci of S. cerevisiae and S. pombe, the regulatory logic that governs the tight control of the key meiosis-inducing genes in these organisms is completely different.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-1502179, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-1592244, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-1671176, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-1682054, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-1936989, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-2196437, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-2247050, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-2500253, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-2900761, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-3034608, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-3280136, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-3821727, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-7926770, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-7969124, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-7975894, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-8177171, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-8178371, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-8227043, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-8303296, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-8339935, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-8455605, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-8548797, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-8848833, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-8945514, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-9062192, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-9118214, http://linkedlifedata.com/resource/pubmed/commentcorrection/9819418-9528770
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0270-7306
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7317-26
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
The mating-type proteins of fission yeast induce meiosis by directly activating mei3 transcription.
pubmed:affiliation
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't