Publication Title

Biochemical and Biophysical Research Communications

Document Type

Article

Department or Program

Chemistry

Second Department or Program

Biochemistry

Publication Date

2-27-2023

Keywords

Borrelia burgdorferi, DNA binding protein, Electrophoretic mobility shift assay (EMSA), RNA binding protein, SpoVG

Abstract

The Borrelia burgdorferi SpoVG protein has previously been found to be a DNA- and RNA-binding protein. To aid in the elucidation of ligand motifs, affinities for numerous RNAs, ssDNAs, and dsDNAs were measured and compared. The loci used in the study were spoVG, glpFKD, erpAB, bb0242, flaB, and ospAB, with particular focus on the untranslated 5′ portion of the mRNAs. Performing binding and competition assays yielded that the 5′ end of spoVG mRNA had the highest affinity while the lowest observed affinity was to the 5’ end of flaB mRNA. Mutagenesis studies of spoVG RNA and ssDNA sequences suggested that the formation of SpoVG-nucleic acid complexes are not entirely dependent on either sequence or structure. Additionally, exchanging uracil for thymine in ssDNAs did not affect protein-nucleic acid complex formation.

Comments

Original version is available from the publisher at: https://doi.org/10.1016/j.bbrc.2023.02.044

PubMed ID

36889033

Copyright Note

© 2023 The Authors.

Required Publisher's Statement

Published by Elsevier Inc. This is an open access article under the CC BY-NC license.

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