Publication Date:
1992-01-10
Description:
Many specific DNA-binding proteins bind to sites with dyad symmetry, and the bound form of the protein is a dimer. For some proteins, dimers form in solution and bind to DNA. LexA repressor of Escherichia coli has been used to test an alternative binding model in which two monomers bind sequentially. This model predicts that a repressor monomer should bind with high specificity to an isolated operator half-site. Monomer binding to a half-site was observed. A second monomer bound to an intact operator far more tightly than the first monomer; this cooperativity arose from protein-protein contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, B -- Little, J W -- GM24178/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):203-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Arizona, Tucson 85721.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553548" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/*metabolism
;
Base Sequence
;
Binding Sites
;
DNA, Bacterial/*metabolism
;
DNA-Binding Proteins/*metabolism
;
Deoxyribonucleases
;
Escherichia coli/*metabolism
;
Kinetics
;
Macromolecular Substances
;
Models, Structural
;
Molecular Sequence Data
;
Oligodeoxyribonucleotides/metabolism
;
Operon
;
Rec A Recombinases/genetics
;
Repressor Proteins/metabolism
;
*Serine Endopeptidases
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
