The DNA-binding domain of two bZIP transcription factors, the Epstein-Barr virus switch gene product EB1 and Jun, is a bipartite nuclear targeting sequence

I Mikaélian, E Drouet, V Marechal, G Denoyel, J C Nicolas, A Sergeant
1993 Journal of Virology  
Cell 63: [341][342][343][344][345][346][347][348][349][350][351] 1990), has been shown to be subject to regulation. We show here that for both EB1 and Jun the nuclear targeting signals (NTS) in the proteins' primary sequences are two clusters of positively charged amino acids. These clusters, called BRA and BRB, are necessary and sufficient to direct 13-galactosidase to the nuclear compartment and act as a bipartite NTS. They are conserved among all the bZIP proteins, and although they are not
more » ... dentical, they probably share the same function. Site-directed mutagenesis studies made on these basic clusters suggest that they also act as a bipartite NTS in the EB1 protein. Our results also demonstrate that in EB1 and Jun, these bipartite NTS are superimposed with bipartite DNA-binding domains, since BRA and BRB are required in vitro for direct and specific contact between these proteins and their DNA-binding sites. 734 on May 8, 2020 by guest
doi:10.1128/jvi.67.2.734-742.1993 fatcat:g3f7qy2klrekvgcrjkvsjlofyi