Quinoxaline Antibiotics Enhance Peptide Nucleic Acid Binding to Double-Stranded DNA†

Biochemistry ◽  
2000 ◽  
Vol 39 (31) ◽  
pp. 9502-9507 ◽  
Author(s):  
Niels Erik Møllegaard ◽  
Christian Bailly ◽  
Michael J. Waring ◽  
Peter E. Nielsen
2005 ◽  
Vol 49 (1) ◽  
pp. 167-168 ◽  
Author(s):  
Toru Sugiyama ◽  
Yasutada Imamura ◽  
Wataru Hakamata ◽  
Masaaki Kurihara ◽  
Atsushi Kittaka

1998 ◽  
Vol 18 (6) ◽  
pp. 3580-3585 ◽  
Author(s):  
Wenjin Zheng ◽  
Stephen Albert Johnston

ABSTRACT Yeast bleomycin hydrolase, Gal6p, is a cysteine peptidase that detoxifies the anticancer drug bleomycin. Gal6p is a dual-function protein capable of both nucleic acid binding and peptide cleavage. We now demonstrate that Gal6p exhibits sequence-independent, high-affinity binding to single-stranded DNA, nicked double-stranded DNA, and RNA. A region of the protein that is involved in binding both RNA and DNA substrates is delineated. Immunolocalization reveals that the Gal6 protein is chiefly cytoplasmic and thus may be involved in binding cellular RNAs. Variant Gal6 proteins that fail to bind nucleic acid also exhibit reduced ability to protect cells from bleomycin toxicity, suggesting that the nucleic acid binding activity of Gal6p is important in bleomycin detoxification and may be involved in its normal biological functions.


2008 ◽  
Vol 372 (4) ◽  
pp. 765-771 ◽  
Author(s):  
Khatcharin Siriwong ◽  
Parawan Chuichay ◽  
Suwipa Saen-oon ◽  
Chaturong Suparpprom ◽  
Tirayut Vilaivan ◽  
...  

2016 ◽  
Vol 52 (42) ◽  
pp. 6930-6933 ◽  
Author(s):  
A. Manicardi ◽  
E. Gyssels ◽  
R. Corradini ◽  
A. Madder

Furan-modified peptide nucleic acid (PNA) probes are able to crosslink to DNA strand after hybridization with complementary ssDNA or after stand displacement in dsDNA.


FEBS Letters ◽  
2012 ◽  
Vol 586 (21) ◽  
pp. 3865-3869 ◽  
Author(s):  
Ji Eun Kim ◽  
Soojin Yoon ◽  
Hyejung Mok ◽  
Woong Jung ◽  
Dong-Eun Kim

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