G-Quadruplex DNA- and RNA-Specific-Binding Proteins Engineered from the RGG Domain of TLS/FUS

2015 ◽  
Vol 10 (11) ◽  
pp. 2564-2569 ◽  
Author(s):  
Kentaro Takahama ◽  
Arisa Miyawaki ◽  
Takumi Shitara ◽  
Keita Mitsuya ◽  
Masayuki Morikawa ◽  
...  
FEBS Journal ◽  
2011 ◽  
Vol 278 (6) ◽  
pp. 988-998 ◽  
Author(s):  
Kentaro Takahama ◽  
Katsuhito Kino ◽  
Shigeki Arai ◽  
Riki Kurokawa ◽  
Takanori Oyoshi

2015 ◽  
Vol 51 (33) ◽  
pp. 7242-7244 ◽  
Author(s):  
Jun Gao ◽  
Boris L. Zybailov ◽  
Alicia K. Byrd ◽  
Wezley C. Griffin ◽  
Shubeena Chib ◽  
...  

DNA binding proteins Sub1 and PC4 preferentially bind to G-quadruplex DNA, providing a new link between DNA metabolism and G4-DNA.


2015 ◽  
Vol 51 (14) ◽  
pp. 2964-2967 ◽  
Author(s):  
Bruno Pagano ◽  
Luigi Margarucci ◽  
Pasquale Zizza ◽  
Jussara Amato ◽  
Nunzia Iaccarino ◽  
...  

Starting from a chemoproteomic-driven approach, novel human telomeric G-quadruplex binding proteins were identified that directly bind the DNA structure in vitro and colocalize with such structures in cells.


RSC Advances ◽  
2018 ◽  
Vol 8 (36) ◽  
pp. 20222-20227 ◽  
Author(s):  
Dongli Li ◽  
Jin-Qiang Hou ◽  
Wei Long ◽  
Yu-Jing Lu ◽  
Wing-Leung Wong ◽  
...  

A significant fluorescent signal enhancement attributed to hydrogen-bonding interactions through the amino groups of a small binding ligand in the G-quartets (binding energy: −6.2 kcal mol−1).


2012 ◽  
Vol 102 (3) ◽  
pp. 15a
Author(s):  
Helen Hwang ◽  
Noah Buncher ◽  
Patricia Opresko ◽  
Sua Myong

RSC Advances ◽  
2018 ◽  
Vol 8 (41) ◽  
pp. 22931-22931
Author(s):  
Dongli Li ◽  
Jin-Qiang Hou ◽  
Wei Long ◽  
Yu-Jing Lu ◽  
Wing-Leung Wong ◽  
...  

Correction for ‘A study on a telo21 G-quadruplex DNA specific binding ligand: enhancing the molecular recognition ability via the amino group interactions’ by Dongli Li et al., RSC Adv., 2018, 8, 20222–20227.


2021 ◽  
Author(s):  
James Edwards-Smallbone ◽  
Anders L Jensen ◽  
Lydia E Roberts ◽  
Francis Isidore Garcia Totanes ◽  
Sarah R Hart ◽  
...  

In the early-diverging protozoan parasite Plasmodium, few telomere-binding proteins have been identified and several are unique. Plasmodium telomeres, like those of most eukaryotes, contain guanine-rich repeats that can form G-quadruplex structures. In model systems, quadruplex-binding drugs can disrupt telomere maintenance and some quadruplex-binding drugs are potent anti-plasmodial agents. Therefore, telomere-interacting and quadruplex-interacting proteins may offer new targets for anti-malarial therapy. Here, we report that P. falciparum GBP2 is such a protein. It was identified via Proteomics of Isolated Chromatin fragments, applied here for the first time in Plasmodium. In vitro, PfGBP2 binds specifically to G-rich telomere repeats in quadruplex form and it can also bind to G-rich RNA. In vivo, PfGBP2 partially colocalises with the known telomeric protein HP1 but is also found in the cytoplasm, probably due to its affinity for RNA. Consistently, its interactome includes numerous RNA-associated proteins. PfGBP2 is evidently a multifunctional DNA/RNA-binding factor in Plasmodium.


2005 ◽  
Vol 12 (10) ◽  
pp. 847-854 ◽  
Author(s):  
Katrin Paeschke ◽  
Tomas Simonsson ◽  
Jan Postberg ◽  
Daniela Rhodes ◽  
Hans Joachim Lipps

Sign in / Sign up

Export Citation Format

Share Document