Isolation and characterization of chicken GA-binding protein.
We have purified and characterized chicken liver nuclear proteins that bind to Ets binding sites (EBSs) of ribosomal protein (r-protein) gene promoters. We employed supershift assays and antibodies to mouse GA binding protein (GABP), to show that the proteins were similar to alpha and beta subunits of GABP. Western blot analysis identified 54- and 38-kDa proteins as the alpha type, and a 46-kDa protein as the beta type. When compared with nuclear extracts (NEs) of other species, we observed that the 38-kDa protein was unique to chicken, and appears to be derived from the 54-kDa protein. The 54- and 46-kDa proteins were highly expressed in chicken tissues and were major components through higher animals, indicating that both proteins have a conserved role.
Toku
Seikichi
S
Department of Biochemistry, School of Medicine, University of the Ryukyus, 207 Uehara, Nishihara, Okinawa 903-0125, Japan. toku@med.u-ryukyu.ac.jp
Quaye
Isaac K E
IK
Tanaka
Tatsuo
T
D000818:Animals; D001665:Binding Sites; D015153:Blotting, Western; D002645:Chickens; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D019143:Evolution, Molecular; D051268:GA-Binding Protein Transcription Factor; D008099:Liver / Q000737:chemistry / Q000378:metabolism*; D009687:Nuclear Proteins / Q000302:isolation & purification / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism*; D014157:Transcription Factors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*
D004268:DNA-Binding Proteins; D051268:GA-Binding Protein Transcription Factor; D009687:Nuclear Proteins; D012269:Ribosomal Proteins; D014157:Transcription Factors