A chronocoulometric LNA sensor for amplified detection of K-ras mutation based on site-specific DNA cleavage of restriction endonuclease

2013 ◽  
Vol 42 ◽  
pp. 409-414 ◽  
Author(s):  
Liqing Lin ◽  
Ailin Liu ◽  
Chengfei Zhao ◽  
Shaohuang Weng ◽  
Yun Lei ◽  
...  
Keyword(s):  
Restriction Endonuclease ◽  
Dna Cleavage ◽  
Site Specific ◽  
Ras Mutation

scholarly journals Ca2+-mediated Site-specific DNA Cleavage and Suppression of Promiscuous Activity of KpnI Restriction Endonuclease

2004 ◽  
Vol 279 (48) ◽  
pp. 49736-49740 ◽  
Author(s):  
Siddamadappa Chandrashekaran ◽  
Matheshwaran Saravanan ◽  
Deshpande R. Radha ◽  
Valakunja Nagaraja
Keyword(s):  
Restriction Endonuclease ◽  
Dna Cleavage ◽  
Site Specific

scholarly journals Site-specific DNA cleavage of synthetic NarL sites by an engineered Escherichia coli NarL protein-1,10-phenanthroline cleaving agent

2008 ◽  
Vol 11 (10) ◽  
pp. 2427-2436 ◽  
Author(s):  
Gaoping Xiao ◽  
Daniel L. Cole ◽  
Robert P. Gunsalus ◽  
David S. Sigman ◽  
Chi-Hong B. Chen
Keyword(s):  
Escherichia Coli ◽  
Dna Cleavage ◽  
Site Specific ◽  
Engineered Escherichia Coli

Functional analysis of box I mutations in yeast site-specific recombinases Flp and R: pairwise complementation with recombinase variants lacking the active-site tyrosine

1992 ◽  
Vol 12 (9) ◽  
pp. 3757-3765
Author(s):  
J W Chen ◽  
B R Evans ◽  
S H Yang ◽  
H Araki ◽  
Y Oshima ◽  
...  
Keyword(s):  
Active Site ◽  
Dna Cleavage ◽  
Substrate Binding ◽  
Point Mutations ◽  
Transfer Reactions ◽  
Strand Transfer ◽  
Site Specific ◽  
Arginine Residues ◽  
Active Site Tyrosine ◽  
Half Site

The site-specific recombinases Flp and R from Saccharomyces cerevisiae and Zygosaccharomyces rouxii, respectively, are related proteins that belong to the yeast family of site-specific recombinases. They share approximately 30% amino acid matches and exhibit a common reaction mechanism that appears to be conserved within the larger integrase family of site-specific recombinases. Two regions of the proteins, designated box I and box II, also harbor a significantly high degree of homology at the nucleotide sequence level. We have analyzed the properties of Flp and R variants carrying point mutations within the box I segment in substrate-binding, DNA cleavage, and full-site and half-site strand transfer reactions. All mutations abolish or seriously diminish recombinase function either at the substrate-binding step or at the catalytic steps of strand cleavage or strand transfer. Of particular interest are mutations of Arg-191 of Flp and R, residues which correspond to one of the two invariant arginine residues of the integrase family. These variant proteins bind substrate with affinities comparable to those of the corresponding wild-type recombinases. Among the binding-competent variants, only Flp(R191K) is capable of efficient substrate cleavage in a full recombination target. However, this protein does not cleave a half recombination site and fails to complete strand exchange in a full site. Strikingly, the Arg-191 mutants of Flp and R can be rescued in half-site strand transfer reactions by a second point mutant of the corresponding recombinase that lacks its active-site tyrosine (Tyr-343). Similarly, Flp and R variants of Cys-189 and Flp variants at Asp-194 and Asp-199 can also be complemented by the corresponding Tyr-343-to-phenylalanine recombinase mutant.

scholarly journals Using Single Molecule Methods to Study Mechanisms of Site Specific DNA Cleavage

2019 ◽  
Vol 116 (3) ◽  
pp. 504a
Author(s):  
Allen C. Price ◽  
Stephen D. Parziale ◽  
Karissa Mehrtens ◽  
Anna D. Ware ◽  
Emily K. Matozel ◽  
...  
Keyword(s):  
Single Molecule ◽  
Dna Cleavage ◽  
Site Specific

Site-Specific DNA Cleavage byChlorellaVirus Topoisomerase II†

Biochemistry ◽  
2002 ◽  
Vol 41 (39) ◽  
pp. 11761-11769 ◽  
Author(s):  
John M. Fortune ◽  
Jennifer S. Dickey ◽  
Oleg V. Lavrukhin ◽  
James L. Van Etten ◽  
R. Stephen Lloyd ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Topoisomerase Ii ◽  
Site Specific
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