Publication Date:
1990-05-18
Description:
The NH2-terminal locations of a dimer containing the DNA binding domain of the yeast transcriptional activator GCN4 have been mapped on the binding sites 5'-CTGACTAAT-3' and 5'-ATGACTCTT-3'. Affinity cleaving was effected by synthetic GCN4 proteins with Fe.EDTA moieties at the NH2-terminus. Analysis of the DNA cleavage patterns for dimers of the Fe.EDTA-proteins corresponding to GCN4 residues 222 to 281 and 226 to 281 revealed that the NH2-termini were in the major groove nine to ten base pairs apart and were symmetrically displaced four to five base pairs from the central C of the recognition site. This result is consistent with the Y-shaped scissor grip-leucine zipper model recently proposed for a class of DNA binding proteins important in the regulation of gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oakley, M G -- Dervan, P B -- New York, N.Y. -- Science. 1990 May 18;248(4957):847-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2111578" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Base Sequence
;
Binding Sites
;
DNA/*metabolism
;
*DNA-Binding Proteins
;
Edetic Acid/metabolism
;
Ferric Compounds/metabolism
;
Fungal Proteins/*metabolism
;
Leucine
;
Macromolecular Substances
;
Molecular Sequence Data
;
Molecular Structure
;
*Protein Kinases
;
*Saccharomyces cerevisiae Proteins
;
Transcription Factors/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink