Phosphorylation at serine 89 induces a shift in gel mobility but has little effect on the function of adenovirus type 5 E1A proteins.
Phosphorylation at serine 89 was shown to be the major cause of the shift in gel migration of the 289R and 243R early region 1A (E1A) proteins of human adenovirus type 5. However, conversion of Ser-89 to alanine by site-directed mutagenesis did not abolish E1A transactivating or transforming activities, suggesting that phosphorylation at this site is not necessary for these E1A functions.
Dumont
D J
DJ
Department of Pathology, McMaster University, Hamilton, Ontario, Canada.
Tremblay
M L
ML
Branton
P E
PE
D017456:Adenovirus Early Proteins; D000260:Adenoviruses, Human / Q000032:analysis* / Q000235:genetics; D001483:Base Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005786:Gene Expression Regulation; D015696:Gene Products, tat; D008969:Molecular Sequence Data; D009856:Oncogene Proteins, Viral / Q000235:genetics / Q000302:isolation & purification* / Q000502:physiology; D010750:Phosphoproteins / Q000302:isolation & purification* / Q000502:physiology; D010766:Phosphorylation; D010768:Phosphoserine; D012694:Serine / Q000031:analogs & derivatives; D014157:Transcription Factors / Q000302:isolation & purification / Q000502:physiology
D017456:Adenovirus Early Proteins; D015696:Gene Products, tat; D009856:Oncogene Proteins, Viral; D010750:Phosphoproteins; D014157:Transcription Factors; D010768:Phosphoserine; D012694:Serine