TY - JOUR
T1 - The Zuo1 C-terminal domain stabilizes DNA guanosine quadruplex (G4) structures located on chromosome IX in Saccharomyces cerevisiae
AU - Burkhart, Ines
AU - Limmer, Michaela
AU - Penedo , J. Carlos
AU - Sauer, Li-Chia
AU - Schwalbe, Harald
AU - Paeschke, Katrin
N1 - Funding: The Fritz Thyssen Stiftung supported this work by a fellowship to K.P. This work has further been supported by the DFG graduate research program CLiC (GRK 1986) and by DFG project (SCHW 701/29-1, 531012774) to I.B. and H.S. KP and CP thank the University of Bonn and the University of St Andrews for a joint grant through their Global Office collaboration programme.
PY - 2025/11/11
Y1 - 2025/11/11
N2 - Deoxyguanosine quadruplexes (G4s) form stable non-B-DNA structures that can affect transcription, replication, and genome stability. Depending on various factors including cation binding, G4s can fold into different topologies, which can be linked to distinct function. In cells, G4 folding, function, and unfolding is affected by proteins that specifically target G4s. Zuo1 is a G4-binding protein in yeast. To investigate Zuo1 binding and its consequences on G4 formation and topology, we characterized Zuo1’s interaction with G4s, both in vitro and in vivo. The C-terminus (Zuo1348-433) of Zuo1 interacts with the G4s. We characterized this interaction by combining nuclear magnetic resonance spectroscopy, single-molecule Förster Resonance Energy Transfer (smFRET), and in vivo experiments with G4IX that is located on yeast chromosome IX. The Zuo1–G4IX interaction stabilizes this G4 structure and triggers conformational shifts depending on the cation environment. The data presented here demonstrate that Zuo1 targets a specific conformation state of G4 IX, modulates G4 toppology.
AB - Deoxyguanosine quadruplexes (G4s) form stable non-B-DNA structures that can affect transcription, replication, and genome stability. Depending on various factors including cation binding, G4s can fold into different topologies, which can be linked to distinct function. In cells, G4 folding, function, and unfolding is affected by proteins that specifically target G4s. Zuo1 is a G4-binding protein in yeast. To investigate Zuo1 binding and its consequences on G4 formation and topology, we characterized Zuo1’s interaction with G4s, both in vitro and in vivo. The C-terminus (Zuo1348-433) of Zuo1 interacts with the G4s. We characterized this interaction by combining nuclear magnetic resonance spectroscopy, single-molecule Förster Resonance Energy Transfer (smFRET), and in vivo experiments with G4IX that is located on yeast chromosome IX. The Zuo1–G4IX interaction stabilizes this G4 structure and triggers conformational shifts depending on the cation environment. The data presented here demonstrate that Zuo1 targets a specific conformation state of G4 IX, modulates G4 toppology.
U2 - 10.1093/nar/gkaf1055
DO - 10.1093/nar/gkaf1055
M3 - Article
SN - 0305-1048
VL - 53
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 20
M1 - gkaf1055
ER -