Sequence-specific binding of HMG-I(Y) to the proximal promoter of the gp91-phox gene.
Screening of a cDNA expression library with a CCAAT-box element derived from the myelomonocyte-specific gp91-phox promoter resulted in the isolation of three independent HMG-I(Y) cDNA clones. Filter binding competition studies reveal that HMG-Y binds to this promoter element in a sequence-specific manner and exhibits a gradient of binding affinities for various A/T-rich sequences. Two adjacent A/T-rich regions within the gp91-phox promoter CCAAT-box element are required for maximal binding. In addition, competition experiments demonstrate that the binding affinity of HMG-Y is influenced by sequences that flank A/T-rich core binding sites.
Skalnik
D G
DG
Division of Hematology/Oncology, Children's Hospital, Dana-Farber Cancer Institute, Boston, MA.
Neufeld
E J
EJ
D001483:Base Sequence; D001665:Binding Sites; D001667:Binding, Competitive; D003001:Cloning, Molecular; D004247:DNA / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006609:High Mobility Group Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009247:NADH, NADPH Oxidoreductases / Q000235:genetics*; D019255:NADPH Oxidases; D011401:Promoter Regions, Genetic
D006609:High Mobility Group Proteins; D004247:DNA; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases