Intramolecular G-quadruplex-hairpin loop structure competition of a GC-rich exon region in the TMPRSS2 gene

2021 ◽  
Author(s):  
Wataru Sugimoto ◽  
Natsuki Kinoshita ◽  
Minori Nakata ◽  
Tatsuya Ohyama ◽  
Hisae Minatojima-Minaminachi ◽  
...  

We identified cytosine-rich regions adjacent to guanine-rich regions in protease genes. A typical GC-rich sequence derived from the TMPRSS2 gene showed structural competition between a G-quadruplex and a hairpin loop,...


2021 ◽  
Vol 14 (2) ◽  
pp. 121
Author(s):  
André Miranda ◽  
Tiago Santos ◽  
Eric Largy ◽  
Carla Cruz

We have designed AS1411-N6, a derivative of the nucleolin (NCL)-binding aptamer AS1411, by adding six nucleotides to the 5′-end that are complementary to nucleotides at the 3′-end forcing it into a stem-loop structure. We evaluated by several biophysical techniques if AS1411-N6 can adopt one or more conformations, one of which allows NCL binding. We found a decrease of polymorphism of G-quadruplex (G4)-forming sequences comparing to AS1411 and the G4 formation in presence of K+ promotes the duplex folding. We also studied the binding properties of ligands TMPyP4, PhenDC3, PDS, 360A, and BRACO-19 in terms of stability, binding, topology maintenance of AS1411-N6, and NCL recognition. The melting experiments revealed promising stabilizer effects of PhenDC3, 360A, and TMPyP4, and the affinity calculations showed that 360A is the most prominent affinity ligand for AS1411-N6 and AS1411. The affinity determined between AS1411-N6 and NCL denoting a strong interaction and complex formation was assessed by PAGE in which the electrophoretic profile of AS1411-N6 showed bands of the dimeric form in the presence of the ligands and NCL.



2015 ◽  
Vol 13 (13) ◽  
pp. 4031-4040 ◽  
Author(s):  
David E. Thurston ◽  
Higia Vassoler ◽  
Paul J. M. Jackson ◽  
Colin H. James ◽  
Khondaker M. Rahman

Pyrrolobenzodiazepine (PBD) monomer GWL-78 reacts faster with DNA hairpins containing a hexaethylene glycol (HEG) loop compared to hairpins containing a TTT loop due to the greater structural flexibility of the HEG.



2002 ◽  
Vol 184 (12) ◽  
pp. 3411-3415 ◽  
Author(s):  
Kohei Goshi ◽  
Tetsuya Uchida ◽  
Alexander Lezhava ◽  
Masayuki Yamasaki ◽  
Keiichiro Hiratsu ◽  
...  

ABSTRACT Cloning and sequencing of the telomere of Streptomyces griseus revealed five palindromic sequences in the terminal 116 nucleotides, all of which can make a hairpin loop structure. However, the end sequence cannot form the foldback secondary structure that is common in Streptomyces telomeres and is suggested to be necessary for terminal replication. Both inside ends of the terminal inverted repeat (TIR) were also cloned and sequenced. The results confirmed the size of the TIR to be 24 kb and identified two almost identical open reading frames that might have been involved in the formation of the TIR.



Author(s):  
Kazumi Hosono ◽  
Hideo Hosaka ◽  
Gota Kawai ◽  
Kazuyuki Takai ◽  
Hiroshi Takaku
Keyword(s):  


1997 ◽  
Vol 17 (5) ◽  
pp. 2649-2657 ◽  
Author(s):  
H Shi ◽  
B E Hoffman ◽  
J T Lis

B52, also known as SRp55, is a member of the Drosophila melanogaster SR protein family, a group of nuclear proteins that are both essential splicing factors and specific splicing regulators. Like most SR proteins, B52 contains two RNA recognition motifs in the N terminus and a C-terminal domain rich in serine-arginine dipeptide repeats. Since B52 is an essential protein and is expected to play a role in splicing a subset of Drosophila pre-mRNAs, its function is likely to be mediated by specific interactions with RNA. To investigate the RNA-binding specificity of B52, we isolated B52-binding RNAs by selection and amplification from a pool of random RNA sequences by using full-length B52 protein as the target. These RNAs contained a conserved consensus motif that constitutes the core of a secondary structural element predicted by energy minimization. Deletion and substitution mutations defined the B52-binding site on these RNAs as a hairpin loop structure covering about 20 nucleotides, which was confirmed by structure-specific enzymatic probing. Finally, we demonstrated that both RNA recognition motifs of B52 are required for RNA binding, while the RS domain is not involved in this interaction.



Virology ◽  
1994 ◽  
Vol 202 (2) ◽  
pp. 1079-1082 ◽  
Author(s):  
Yanping Zhang ◽  
Peter Strasser ◽  
Reingard Grabherr ◽  
James L. Van Etten


Biochemistry ◽  
2003 ◽  
Vol 42 (40) ◽  
pp. 11736-11744 ◽  
Author(s):  
Wei Li ◽  
Daisuke Miyoshi ◽  
Shu-ichi Nakano ◽  
Naoki Sugimoto


2016 ◽  
Vol 138 (8) ◽  
pp. 2563-2570 ◽  
Author(s):  
Buket Onel ◽  
Megan Carver ◽  
Guanhui Wu ◽  
Daria Timonina ◽  
Salil Kalarn ◽  
...  
Keyword(s):  


2016 ◽  
Author(s):  
Buket Onel ◽  
Guanhui Wu ◽  
Megan Carver ◽  
Daria Timonina ◽  
Marti Larriva ◽  
...  
Keyword(s):  


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