The phosphorylated forms of the transcription factor, Egr-1, bind to DNA more efficiently than non-phosphorylated.
The transcription factor, Early growth response-1, Egr-1, occurs in several forms differing in length due to three alternate translation start sites (1). Egr-1 has also been reported to be phosphorylated although a role for this modification is unknown. Using dephosphorylation and hyperphosphorylation studies, we show here that phosphorylated Egr-1 is much more efficiently bound to its DNA binding element (GCE) and binds in a dose-dependent fashion. Egr-1 plays complex roles in growth regulation and we suggest that alternate forms of phosphorylated Egr-1 may account for this.
Huang
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RP
La Jolla Cancer Research Foundation, Ca 92037.
Adamson
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D000818:Animals; D016367:Baculoviridae; D001665:Binding Sites; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D009036:Moths; D010750:Phosphoproteins / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012045:Regulatory Sequences, Nucleic Acid; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000378:metabolism*; D016335:Zinc Fingers
D004268:DNA-Binding Proteins; D010750:Phosphoproteins; D011994:Recombinant Proteins; D014157:Transcription Factors; D004247:DNA