A multiplicity of CCAAT box-binding proteins
Identifieur interne : 002511 ( Istex/Corpus ); précédent : 002510; suivant : 002512A multiplicity of CCAAT box-binding proteins
Auteurs : Arnulf Dorn ; Jacques Bollekens ; Adrian Staub ; Christophe Benoist ; Diane MathisSource :
- Cell [ 0092-8674 ] ; 1987.
English descriptors
- Teeft :
- Antisense, Antisense strand, Antisense strands, Arrows point, Assay, Band intensity, Binding, Binding core, Binding efficiency, Binding properties, Binding proteins, Binding reaction, Binding requirements, Binding site, Biol, Ccaat, Ccaat boxes, Ccaat protein, Ccaat proteins, Ccaat sequence, Ccaat sequences, Chicken liver, Cleavage, Cleavage products, Competition experiments, Complex formation, Contact sites, Different entities, Distinct proteins, Dna, Dnaase, Dorn, Element harbors, Ethanol precipitation, Experimental evidence, Fetal haemoglobin, Fragment, Functional relevance, Gene, Gene expression, Gene promoters, Good correlation, Heat shock transcription factor, Hela, Hela cell, Hela cells, Kelly, Major histocompatibility, Mcknight, Methylated, Methylation, Methylation interference, Methylation interference mapping, Mouse promoter, Murine, Murine class, Mutagenesis, Mutation, Neutral polyacrylamide, Nuclear protein, Nuclear proteins, Nucleotide, Oligo, Oligonucleotide, Oligonucleotides, Oligos, Other hand, Other oligonucleotides, Point mutation, Polyacrylamide, Promoter, Promoter fragment, Promoter function, Promoter region, Purine contacts, Random sequence, Relative binding efficiencies, Retardation, Retardation assay, Retardation assays, Retarded band, Room temperature, Same protein, Saturation mutagenesis, Saturation mutagenesis experiment, Sense strand, Sequence elements, Sequencing, Specific binding, Thymidine kinase promoter, Tjian, Transcription, Transcription factor, Transcriptional, Transcriptional control elements, Typical binding reaction, Unlabeled, Unlabeled competitor oligonucleotide.
Abstract
Abstract: NF-Y is a sequence-specific DNA-binding protein that recognizes the Y box, a promoter element common to all major histocompatibility complex class II genes. Since the 14-base Y element harbors a CCAAT box in reverse, we were prompted to ask whether NF-Y is actually a CCAAT box-binding protein and whether it is related to the previously described CCAAT-binding factors CBP and CTF/NF-I. Data from gel retardation, methylation interference, saturation mutagenesis, and cross-competition experiments establish definitively that NF-Y is an entirely distinct CCAAT box-binding entity. Moreover, these experiments have uncovered a fourth CCAAT-binding protein, NF-Y∗, that interacts with the thymidine kinase promoter. Clearly, then, there exists a multiplicity of factors that recognize CCAAT sequences; it now becomes imperative to understand the functional significance of this multiplicity.
Url:
DOI: 10.1016/0092-8674(87)90513-7
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Abstract: NF-Y is a sequence-specific DNA-binding protein that recognizes the Y box, a promoter element common to all major histocompatibility complex class II genes. Since the 14-base Y element harbors a CCAAT box in reverse, we were prompted to ask whether NF-Y is actually a CCAAT box-binding protein and whether it is related to the previously described CCAAT-binding factors CBP and CTF/NF-I. Data from gel retardation, methylation interference, saturation mutagenesis, and cross-competition experiments establish definitively that NF-Y is an entirely distinct CCAAT box-binding entity. Moreover, these experiments have uncovered a fourth CCAAT-binding protein, NF-Y∗, that interacts with the thymidine kinase promoter. Clearly, then, there exists a multiplicity of factors that recognize CCAAT sequences; it now becomes imperative to understand the functional significance of this multiplicity.</div>
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<abstract>Abstract: NF-Y is a sequence-specific DNA-binding protein that recognizes the Y box, a promoter element common to all major histocompatibility complex class II genes. Since the 14-base Y element harbors a CCAAT box in reverse, we were prompted to ask whether NF-Y is actually a CCAAT box-binding protein and whether it is related to the previously described CCAAT-binding factors CBP and CTF/NF-I. Data from gel retardation, methylation interference, saturation mutagenesis, and cross-competition experiments establish definitively that NF-Y is an entirely distinct CCAAT box-binding entity. Moreover, these experiments have uncovered a fourth CCAAT-binding protein, NF-Y∗, that interacts with the thymidine kinase promoter. Clearly, then, there exists a multiplicity of factors that recognize CCAAT sequences; it now becomes imperative to understand the functional significance of this multiplicity.</abstract>
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<ref_bibl><json:string>Bienz and Pelham, 1988</json:string>
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