TY - JOUR
T1 - Quantitative analyses of interactions between SpoVG and RNA/DNA
AU - Saylor, Timothy C.
AU - Savage, Christina R.
AU - Krusenstjerna, Andrew C.
AU - Jusufovic, Nerina
AU - Zückert, Wolfram R.
AU - Brissette, Catherine A.
AU - Motaleb, Md
AU - Schlax, Paula J.
AU - Stevenson, Brian
N1 - Publisher Copyright:
© 2023 The Authors
PY - 2023/4/30
Y1 - 2023/4/30
N2 - 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.
AB - 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.
KW - Borrelia burgdorferi
KW - DNA binding protein
KW - Electrophoretic mobility shift assay (EMSA)
KW - RNA binding protein
KW - SpoVG
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U2 - 10.1016/j.bbrc.2023.02.044
DO - 10.1016/j.bbrc.2023.02.044
M3 - Article
C2 - 36889033
AN - SCOPUS:85149781000
SN - 0006-291X
VL - 654
SP - 40
EP - 46
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
ER -