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Updated: Sep 26, 2025

An Assay for Quantifying Protein-RNA Binding in Bacteria
Published on: June 12, 2019
Solid state NMR chemical shift assignment of the non-structural single-stranded DNA binding protein gVp from fd
Roni Rene Hassid1, Smadar Kedem1, Meital Bachar-Beck1
1School of Chemistry, Tel Aviv University, 6997801, Tel Aviv, Israel.
Abstract:
The non-structural gene V protein (pV, gVp) from fd virus is a non-specific single-stranded DNA binding protein. The role of gVp is to sequester the single-stranded DNA thus reducing the generation of the replicative DNA form and leading to the formation of progeny phage. In this study, we assigned the 13C and 15N resonances of the crystalline unbound protein by magic-angle spinning solid-state NMR. The secondary structure predicted by the NMR shifts is in excellent agreement with the X-ray structure of the same 87-residue protein.
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