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Zinc ions stimulate the cooperative RNA binding of hordeiviral γb protein
Author(s) -
Rakitina Daria V.,
Yelitalia E.,
Kalinitalia O.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.032
Subject(s) - zinc finger , cooperativity , oligonucleotide , rna , cooperative binding , rna binding protein , chemistry , rna recognition motif , structural motif , nucleic acid , biochemistry , coiled coil , zinc , biology , binding site , transcription factor , dna , gene , organic chemistry
A small regulatory γb 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 γb 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 γb 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.