A TATA-box-binding protein binds single-stranded DNA in two modes: To poly(G) tracts and to flexible DNA regions.

ABSTRACT: The TATA-box-binding protein (TBP) homolog from Giardia intestinalis (gTBP) is highly divergent, lacking key phenylalanine residues crucial for binding and unwinding double-stranded DNA. Surprisingly, we determined that gTBP exhibits unconventional DNA-binding properties and preferentially binds to single-stranded DNA (ssDNA) using a DNA-binding pocket that is narrower relative to other eukaryotic TBPs. Additionally, we showed that gTBP binds in two distinct modes, which we call the A and B modes, that are dependent on ssDNA sequence and protein concentration. For the A mode, gTBP binds as an oligomer to ssDNA that contains four or more consecutive guanine bases. For the B mode, using base stacking energy potentials between adjacent dinucleotides as a simple proxy for per-nucleotide flexib

SUBMITTER: Freitag K 

PROVIDER: S-EPMC12209930 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature