Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1992-11-19
pubmed:abstractText
While all basic region/helix-loop-helix (bHLH) proteins bind the consensus CANNTG motif, other factors must be involved in determining regulatory specificity. In this report we show that bases outside this core 6 bp are involved in determining the specificity of binding. Thus, binding of the yeast bHLH protein PHO4, but not CPF-1, is inhibited by the presence of a T residue immediately 5' to their common CACGTG recognition sequence. PHO4 binding specificity is altered by mutation at any of three different positions in the basic region, including a single Glu to Asp substitution. The significance of these data for DNA-binding and transcription regulation by the bHLH family of transcription factors is discussed.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1312255, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1549123, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1731330, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1734524, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1773060, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1827916, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1840505, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1861859, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1944532, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-1987636, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2006410, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2057354, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2068097, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2115126, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2174572, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2183025, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2185892, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2188087, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2220078, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2249662, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2249772, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2251503, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2338243, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2493990, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-2664469, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-3011600, http://linkedlifedata.com/resource/pubmed/commentcorrection/1327757-3915785
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4103-9
pubmed:dateRevised
2010-9-7
pubmed:meshHeading
pubmed-meshheading:1327757-Amino Acid Sequence, pubmed-meshheading:1327757-Base Sequence, pubmed-meshheading:1327757-Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, pubmed-meshheading:1327757-Binding Sites, pubmed-meshheading:1327757-DNA-Binding Proteins, pubmed-meshheading:1327757-Fungal Proteins, pubmed-meshheading:1327757-Genes, Fungal, pubmed-meshheading:1327757-Methionine, pubmed-meshheading:1327757-Molecular Sequence Data, pubmed-meshheading:1327757-Mutagenesis, Site-Directed, pubmed-meshheading:1327757-Oligonucleotide Probes, pubmed-meshheading:1327757-Phosphoric Monoester Hydrolases, pubmed-meshheading:1327757-Protein Conformation, pubmed-meshheading:1327757-Saccharomyces cerevisiae, pubmed-meshheading:1327757-Saccharomyces cerevisiae Proteins, pubmed-meshheading:1327757-Sequence Homology, Nucleic Acid, pubmed-meshheading:1327757-Transcription Factors
pubmed:year
1992
pubmed:articleTitle
Single amino acid substitutions alter helix-loop-helix protein specificity for bases flanking the core CANNTG motif.
pubmed:affiliation
Marie Curie Research Institute, Oxted, Surrey, UK.
pubmed:publicationType
Journal Article, Comparative Study