Publication Date:
2003-06-14
Description:
In eukaryotes, the combinatorial association of sequence-specific DNA binding proteins is essential for transcription. We have used protein arrays to test 492 pairings of a nearly complete set of coiled-coil strands from human basic-region leucine zipper (bZIP) transcription factors. We find considerable partnering selectivity despite the bZIPs' homologous sequences. The interaction data are of high quality, as assessed by their reproducibility, reciprocity, and agreement with previous observations. Biophysical studies in solution support the relative binding strengths observed with the arrays. New associations provide insights into the circadian clock and the unfolded protein response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newman, John R S -- Keating, Amy E -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2097-101. Epub 2003 Jun 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12805554" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Basic-Leucine Zipper Transcription Factors
;
Chromatography, High Pressure Liquid
;
Circadian Rhythm
;
Circular Dichroism
;
Cyclic AMP Response Element-Binding Protein/chemistry/metabolism
;
DNA-Binding Proteins/chemistry/isolation & purification/*metabolism
;
Dimerization
;
G-Box Binding Factors
;
Humans
;
*Leucine Zippers
;
Peptides/chemistry/isolation & purification/metabolism
;
*Protein Array Analysis
;
Protein Binding
;
Protein Folding
;
Protein Structure, Tertiary
;
Signal Transduction
;
Temperature
;
Thermodynamics
;
Transcription Factors/*chemistry/isolation & purification/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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