Adenovirus E1A makes two distinct contacts with the retinoblastoma protein

N Dyson, P Guida, C McCall, E Harlow
1992 Journal of Virology  
Two regions near the amino terminus of the adenovirus EIA protein, which were first identified by sequence conservation among various adenovirus serotypes, have been shown by genetic studies to be essential for ElA-mediated transformation. These same regions are also required for interaction with a number of cellular proteins, including the retinoblastoma protein (pRB). Using synthetic peptides corresponding to portions of these conserved regions, we show that each region can bind independently
more » ... bind independently to pRB. These interactions were observed in both competition and binding assays. In both types of assay, region 2 peptides (ElA amino acids 115 to 132) bound pRB with higher affinity than did region 1 peptides (ElA amino acids 37 to 54), while a peptide combining region 1 and 2 sequences consistently provided the highest-affinity interaction. Crossblocking experiments using region 1 peptides and region 2 peptides suggested that these two regions of ElA make distinct contacts with pRB. These data support the notion that the pRB-binding domain of ElA contains at least two functional elements.
doi:10.1128/jvi.66.7.4606-4611.1992 fatcat:g23h64eiuve7rlgqus26j2moru