Structural highlights
Function
T3RE_ECOLX A type III restriction enzyme that recognizes 2 inversely oriented double-stranded sequences 5'-CAGCAG-3' and cleaves DNA 25-27 base pairs downstream of one site. DNA restriction requires both the Res and Mod subunits (PubMed:11178902, PubMed:15464603). DNA topology affects its action; relaxed and negatively supercoiled DNA are digested but positively supercoiled DNA is not a good substrate (PubMed:11178902). Interacts with DNA approximately one half-turn downstream of the recognition site (PubMed:26067164). After binding to one recognition site undergoes random one-dimensional diffusion along DNA until it collides with a stationary enzyme bound to the second DNA site, which is when DNA cleavage occurs (Probable).[1] [2] [3] [4]
References
- ↑ Janscak P, Sandmeier U, Szczelkun MD, Bickle TA. Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I. J Mol Biol. 2001 Feb 23;306(3):417-31. PMID:11178902 doi:10.1006/jmbi.2000.4411
- ↑ Möncke-Buchner E, Mackeldanz P, Krüger DH, Reuter M. Overexpression and affinity chromatography purification of the Type III restriction endonuclease EcoP15I for use in transcriptome analysis. J Biotechnol. 2004 Oct 19;114(1-2):99-106. PMID:15464603 doi:10.1016/j.jbiotec.2004.06.014
- ↑ Gupta YK, Chan SH, Xu SY, Aggarwal AK. Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I. Nat Commun. 2015 Jun 12;6:7363. doi: 10.1038/ncomms8363. PMID:26067164 doi:https://dx.doi.org/10.1038/ncomms8363
- ↑ Gupta YK, Chan SH, Xu SY, Aggarwal AK. Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I. Nat Commun. 2015 Jun 12;6:7363. doi: 10.1038/ncomms8363. PMID:26067164 doi:https://dx.doi.org/10.1038/ncomms8363
