2009
DOI: 10.1134/s0006297909130033
|View full text |Cite
|
Sign up to set email alerts
|

Nicking endonucleases

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
27
0

Year Published

2011
2011
2022
2022

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 33 publications
(29 citation statements)
references
References 44 publications
1
27
0
Order By: Relevance
“…1) over the 7-mer (cleavage at 5th position to the 5′-end from the recognition site, Fig. 1) in the case of bottom-strand hydrolysis by ss.BspD6I of 26 bp duplex I-E that is consistent with the previous studies [13,26].…”
Section: Resultssupporting
confidence: 92%
“…1) over the 7-mer (cleavage at 5th position to the 5′-end from the recognition site, Fig. 1) in the case of bottom-strand hydrolysis by ss.BspD6I of 26 bp duplex I-E that is consistent with the previous studies [13,26].…”
Section: Resultssupporting
confidence: 92%
“…On the other hand, double-stranded DNA-specific nicking endonucleases are usually monomeric, with the exception of several structure-specific nicking endonucleases , Komori, et al, 2002. For example, the following linear double-stranded DNA-specific nicking endonucleases are all monomeric proteins (Table 1): N-type nicking endonucleases (e.g, N. BspQI), sequence-specific nicking endonucleases naturally or artificially created by mutating restriction enzymes to lose their dimerization ability (Higgins, et al, 2001, Roberts, et al, 2003, Xu, et al, 2001, Yunusova, et al, 2006, Zheleznaya, et al, 2009); V-type nicking endonucleases (e.g., E. coli Vsr), a short patch MMR nicking endonuclease ; Type I DNA topoisomerases (e.g., E. coli Topo I), an enzyme with a supercoil-relaxing activity (Kirkegaard, et al, 1978); retrotransposon-targeting endonucleases (e.g., L1 endonuclease), a site-specific nicking endonuclease that directs the invasion of the retrotransposon (Feng, et al, 1996, Feng, et al, 1998, Maita, et al, 2007, Weichenrieder, et al, 2004; bovine DNase I, a non-specific nicking endonuclease that functions in the host defense (Suck, et al, 1988); E. coli MutH (Ban, et al, 1998), the MMR nicking endonuclease; bacterial UvrC (Nazimiec, et al, 2001), a nucleotide excision repair nicking endonuclease; bacterial endonuclease V (Dalhus, et al, 2009), a deaminated DNAspecific nicking endonuclease; and bacterial and eukaryotic AP endonucleases (Hosfield, et al, 1999, Mol, et al, 2000, an abasic site-specific nicking endonuclease. Known DNA repair systems other than MMR all adopt a monomeric nicking endonuclease to introduce the entry point for the excision reaction.…”
Section: Bacterial Mutl Is a Homodimeric Nicking Endonucleasementioning
confidence: 99%
“…However, unlike REs, nicking endonucleases cleave only one DNA strand. Depending on the strand (top or bottom) nicked, these are designated as "Nt" or "Nb", respectively (Zheleznaya et al 2009). They can be bona fide nicking enzymes, such as frequent cutter Nt.Cvi-PII (Chan et al 2004) and Nt.CviQII (Chan et al 2006) or rare-cutting homing endonucleases (HEases) I-BasI and IHmuI, both of which recognize a degenerate 24-bp sequence (Chan et al 2011).…”
Section: Introductionmentioning
confidence: 99%