Zinc ions stimulate the cooperative RNA binding of hordeiviral gammab protein.
A small regulatory gammab protein of the Poa semilatent hordeivirus (PSLV) contains two zinc finger-like motifs separated by a basic motif in the N-terminal part and a C-terminal coiled-coil motif. Interactions of the recombinant PSLV gammab protein and its mutants with various RNAs (ssRNA, dsRNA, ssRNA oligonucleotides) and ssDNA were studied in gel-shift assays. The results demonstrated that zinc ions are essential for effective nucleic-acid-binding activity of the gammab protein, suggesting the important role of zinc finger motifs in these interactions. Deletion of the C-proximal coiled-coil region did not affect highly cooperative RNA-protein binding, indicating that the N-terminal part of the protein contributes to the protein-protein interactions needed for the protein-RNA cooperativity.
Rakitina
Daria V
DV
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia.
Yelina
Natalia E
NE
Kalinina
Natalia O
NO
D000595:Amino Acid Sequence; D024202:Electrophoretic Mobility Shift Assay; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D009841:Oligonucleotides / Q000378:metabolism; D010942:Plant Viruses / Q000378:metabolism*; D011485:Protein Binding; D012367:RNA, Viral / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism*
D050505:Mutant Proteins; D009841:Oligonucleotides; D012367:RNA, Viral; D011994:Recombinant Proteins; D014764:Viral Proteins; D015032:Zinc