Q Zhang1, K Harada, H S Cho, A D Frankel, D E Wemmer. 1. Department of Chemistry MC-1460, University of California, and Physical Biosciences, Lawrence Berkeley National Laboratory, CA 94720, USA.
Abstract
INTRODUCTION: The RSG-1.2 peptide was selected for specific binding to the Rev response element RNA, as the natural Rev peptide does. The RSG-1.2 sequence has features incompatible with the helical structure of the bound Rev peptide, indicating that it must bind in a different conformation. RESULTS: The binding of the RSG-1.2 peptide to the Rev response element RNA was characterized using multinuclear, multidimensional NMR. The RSG-1.2 peptide is shown to bind with the N-terminal segment of the peptide along the major groove in an extended conformation and turn preceding a C-terminal helical segment, which crosses the RNA groove in the region widened by the presence of purine-purine base pairs. These features make the details of the bound state rather different than that of the Rev peptide which targets the same RNA sequence binding as a single helix along the groove axis. CONCLUSIONS: These studies further demonstrate the versatility of arginine-rich peptides in recognition of specific RNA elements and the lack of conserved structural features in the bound state.
INTRODUCTION: The RSG-1.2 peptide was selected for specific binding to the Rev response element RNA, as the natural Rev peptide does. The RSG-1.2 sequence has features incompatible with the helical structure of the bound Rev peptide, indicating that it must bind in a different conformation. RESULTS: The binding of the RSG-1.2 peptide to the Rev response element RNA was characterized using multinuclear, multidimensional NMR. The RSG-1.2 peptide is shown to bind with the N-terminal segment of the peptide along the major groove in an extended conformation and turn preceding a C-terminal helical segment, which crosses the RNA groove in the region widened by the presence of purine-purine base pairs. These features make the details of the bound state rather different than that of the Rev peptide which targets the same RNA sequence binding as a single helix along the groove axis. CONCLUSIONS: These studies further demonstrate the versatility of arginine-rich peptides in recognition of specific RNA elements and the lack of conserved structural features in the bound state.
Authors: Ashley N Peralta; Yumin Dai; Chringma Sherpa; Stuart F J Le Grice; Webster L Santos Journal: Methods Enzymol Date: 2019-05-15 Impact factor: 1.600
Authors: Yumin Dai; Ashley N Peralta; Jessica E Wynn; Chringma Sherpa; Hao Li; Astha Verma; Stuart F J Le Grice; Webster L Santos Journal: Bioorg Med Chem Date: 2019-03-07 Impact factor: 3.641