The complex formed between the human papillomavirus type 16 E6 protein
and human E6-associated protein, which combine to ubiquitylate and de
grade p53, has been studied bg chemical crosslinking. Analysis of the
interactions of proteins purified from Escherichia coli as wen as prot
eins expressed in insect cells indicates that, while E6 has the capaci
ty to form dimers, E6 and E6-associated protein interact as two monome
rs to form a heterologous dimer. (C) 1997 Federation of European Bioch
emical Societies.