TAILIEUCHUNG - Báo cáo khoa học: Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein Structural modularity, intrinsic disorder and phosphorylation of human papillomavirus E7

DNA tumor viruses ensure genome amplification by hijacking the cellular replication machinery and forcing infected cells to enter the S phase. The retinoblastoma (Rb) protein controls the G1⁄S checkpoint, and is targeted by several viral oncoproteins, among these the E7 protein from human papillomaviruses (HPVs). | ỊFEBS Journal Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein Structural modularity intrinsic disorder and phosphorylation of human papillomavirus E7 Lucia B. Chemes Ignacio E. Sanchez Clara Smal and Gonzalo de Prat-Gay Protein Structure-Function and Engineering Laboratory Fundacion Instituto Leloir and IIBBA-CONICET Buenos Aires Argentina Keywords LxCxE motif natively unfolded proteins phosphorylation retinoblastoma protein viral oncoprotein Correspondence Gonzalo de Prat-Gay Protein StructureFunction and Engineering Laboratory Fundacion Instituto Leloir and IIBBA-CONICET Av. Patricias Argentinas 435 1405 Buenos Aires Argentina Fax 54 11 5238 7501 Tel 54 11 5238 7500 ext. 3209 E-mail gpg@ Received 16 November 2009 revised 4 December 2009 accepted 7 December 2009 doi DNA tumor viruses ensure genome amplification by hijacking the cellular replication machinery and forcing infected cells to enter the S phase. The retinoblastoma Rb protein controls the G1 S checkpoint and is targeted by several viral oncoproteins among these the E7 protein from human papillomaviruses HPVs . A quantitative investigation of the interaction mechanism between the HPV16 E7 protein and the RbAB domain in solution revealed that 90 of the binding energy is determined by the LxCxE motif with an additional binding determinant kcal-mol-1 located in the C-terminal domain of E7 establishing a dual-contact mode. The stoichiometry and subnanomolar affinity of E7 indicated that it can bind RbAB as a monomer. The low-risk HPV11 E7 protein bound kcal-mol-1 more weakly than the high-risk HPV16 and HPV18 type counterparts but the modularity and binding mode were conserved. Phosphorylation at a conserved casein kinase II site in the natively unfolded N-terminal domain of E7 affected the local conformation by increasing the polyproline II content and stabilizing an extended conformation which allowed for a

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