Cosson Bertrand, Berkova Nadia, Couturier Anne, Chabelskaya Svetlana, Philippe Michel, Zhouravleva Galina
Université de Rennes 1, CNRS UMR 6061, IFR 97, avenue du professeur Leon Bernard, 35043 Rennes cedex, France.
Biol Cell. 2002 Sep;94(4-5):205-16. doi: 10.1016/s0248-4900(02)01194-2.
An interaction between human poly(A)-binding protein (PABP) et human eRF3 has been demonstrated using a double-hybrid approach and in vitro assays. Here, we show that the binding of both proteins is conserved through evolution. We also demonstrate that the last 39 C-terminal amino acids of PABP contain the interface that interacts with eRF3. This region includes helix 5, identified by RMN, which is conserved in all known PABPs. Lastly, we demonstrate that eRF3 et PABP molecules interact in vivo.
利用双杂交方法和体外试验已证明人多聚腺苷酸结合蛋白(PABP)与人eRF3之间存在相互作用。在此,我们表明这两种蛋白质的结合在进化过程中是保守的。我们还证明PABP的最后39个C端氨基酸包含与eRF3相互作用的界面。该区域包括通过核磁共振鉴定的螺旋5,在所有已知的PABP中都是保守的。最后,我们证明eRF3和PABP分子在体内相互作用。