Title
Organization of the BcgI restriction-modification protein for the cleavage of eight phosphodiester bonds in DNA Organization of the BcgI restriction-modification protein for the cleavage of eight phosphodiester bonds in DNA
Author
Faculty/Department
Faculty of Sciences. Chemistry
Publication type
article
Publication
London ,
Subject
Chemistry
Source (journal)
Nucleic acids research. - London
Volume/pages
41(2013) :1 , p. 391-404
ISSN
0305-1048
ISI
000312889900064
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
Type IIB restriction-modification systems, such as BcgI, feature a single protein with both endonuclease and methyltransferase activities. Type IIB nucleases require two recognition sites and cut both strands on both sides of their unmodified sites. BcgI cuts all eight target phosphodiester bonds before dissociation. The BcgI protein contains A and B polypeptides in a 2:1 ratio: A has one catalytic centre for each activity; B recognizes the DNA. We show here that BcgI is organized as A2B protomers, with B at its centre, but that these protomers self-associate to assemblies containing several A2B units. Moreover, like the well known FokI nuclease, BcgI bound to its site has to recruit additional protomers before it can cut DNA. DNA-bound BcgI can alternatively be activated by excess A subunits, much like the activation of FokI by its catalytic domain. Eight A subunits, each with one centre for nuclease activity, are presumably needed to cut the eight bonds cleaved by BcgI. Its nuclease reaction may thus involve two A2B units, each bound to a recognition site, with two more A2B units bridging the complexes by proteinprotein interactions between the nuclease domains.
Full text (open access)
https://repository.uantwerpen.be/docman/irua/a4d797/2040c603.pdf
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