Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-5-6
pubmed:databankReference
pubmed:abstractText
The PKC1 gene product, protein kinase C, regulates a mitogen-activated protein kinase (MAPK) cascade, which is implicated in cell wall metabolism. Previously, we identified the pkc1-4 allele in a screen for mutants with increased rates of recombination, indicating that PKC1 may also regulate DNA metabolism. The pkc1-4 allele also conferred a temperature-sensitive (ts) growth defect. Extragenic suppressors were isolated that suppress both the ts and hyperrecombination phenotypes conferred by the pkc1-4 mutation. Eight of these suppressors for into two complementation groups, designated KCS1 and KCS2. KCS1 was cloned and found to encode a novel protein with homology to the basic leucine zipper family of transcription factors. KCS2 is allelic with PTC1, a previously identified type 2C serine/threonine protein phosphatase. Although mutation of either KCS1 or PTC1 causes little apparent phenotype, the kcs1 delta ptc1 delta double mutant fails to grow at 30 degrees. Furthermore, the ptc1 deletion mutation is synthetically lethal in combination with a mutation in MPK1, which encodes a MAPK homologue proposed to act in the PKC1 pathway. Because PTC1 was initially isolated as a component of the Hog1p MAPK pathway, it appears that these two MAPK cascades share a common regulatory feature.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-1195397, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-13433590, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-1406668, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-1411571, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-1729597, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-1819504, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-2196995, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-2253890, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-3327750, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-3469660, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-6280875, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-6310324, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-6336730, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-7681220, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8065337, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8152414, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8183345, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8196609, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8290957, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8306972, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8321321, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8386319, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8386320, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8395005, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8395014, http://linkedlifedata.com/resource/pubmed/commentcorrection/8601473-8504253
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carboxy-Lyases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PTC1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Phosphate..., http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/phosphoribosylaminoimidazole..., http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase 2C
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0016-6731
pubmed:author
pubmed:issnType
Print
pubmed:volume
141
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1275-85
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8601473-Alleles, pubmed-meshheading:8601473-Amino Acid Sequence, pubmed-meshheading:8601473-Base Sequence, pubmed-meshheading:8601473-Carboxy-Lyases, pubmed-meshheading:8601473-Cloning, Molecular, pubmed-meshheading:8601473-Fungal Proteins, pubmed-meshheading:8601473-Genetic Complementation Test, pubmed-meshheading:8601473-Leucine Zippers, pubmed-meshheading:8601473-Molecular Sequence Data, pubmed-meshheading:8601473-Mutation, pubmed-meshheading:8601473-Phenotype, pubmed-meshheading:8601473-Phosphoprotein Phosphatases, pubmed-meshheading:8601473-Phosphotransferases (Phosphate Group Acceptor), pubmed-meshheading:8601473-Protein Kinase C, pubmed-meshheading:8601473-Protein Phosphatase 2, pubmed-meshheading:8601473-RNA, Messenger, pubmed-meshheading:8601473-Recombination, Genetic, pubmed-meshheading:8601473-Saccharomyces cerevisiae, pubmed-meshheading:8601473-Saccharomyces cerevisiae Proteins
pubmed:year
1995
pubmed:articleTitle
Suppressors of a Saccharomyces cerevisiae pkc1 mutation identify alleles of the phosphatase gene PTC1 and of a novel gene encoding a putative basic leucine zipper protein.
pubmed:affiliation
Institute of Cancer Research, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't