A Cysteine-Rich Motif in Poliovirus Protein 2C ATPase Is Involved in RNA Replication and Binds Zinc In Vitro

• DOI: 10.1128/jvi.74.1.334-343.2000
• Publication Date: 2009-04-23T21:08:16Z
• Authors: Thomas Pfister; Keith W. Jones; Eckard Wimmer
• Keywords: Structural motif; Sequence motif

ABSTRACT Protein 2C ATPase of picornaviruses is involved in the rearrangement host cell organelles, viral RNA replication, and encapsidation. However, biochemical molecular mechanisms by which engages these processes are not known. To characterize functional domains , we have focused on a cysteine-rich motif near carboxy terminus poliovirus . This region, well conserved among enteroviruses rhinoviruses displaying an amino acid arrangement resembling zinc finger motifs, was studied genetic analyses. A mutation that replaced first cysteine residue with serine lethal. mutant virus lacked second four potential coordination sites for temperature sensitive. At restrictive temperature, replication inhibited whereas translation polyprotein processing, assayed vitro vivo, appeared to be normal. An intragenomic second-site revertant reinserted missing site recovered at isolated. The sufficient bind vitro, as assessed presence 4-(2-pyridylazo)resorcinol colorimetric assay. Zinc binding, however, required hydrolysis ATP. its precursors 2BC P2 were found exist reduced form poliovirus-infected cells.