![]() NotI may represent an evolutionary intermediate between mobile endonucleases (which recognize longer target sites) and canonical restriction endonucleases. While recognition of the central six base pairs of the target is accomplished via a saturated hydrogen bond network typical of restriction enzymes, the most peripheral base pairs are engaged in a single direct contact in the major groove, reflecting reduced pressure to recognize those positions. This domain positions nearby protein elements for DNA recognition, and serves a structural role. NotI contains a unique metal binding fold, found in a variety of putative endonucleases, occupied by an iron atom coordinated within a tetrahedral Cys4 motif. Because of its specificity (recognizing a site that occurs once per 65 kb), NotI is used to generate large genomic fragments and to map DNA methylation status. radiodurans is suggested.The structure of the rare-cutting restriction endonuclease NotI, which recognizes the 8 bp target 5′-GCGGCCGC-3′, has been solved with and without bound DNA. Thus, drFtsK role in maintaining the normal ge-nome phenotype and cell division in D. The molecular weight is 43.3 kDa, with the recognition site at GCGGCCGC. In vivo drFtsK is dynamic, forms foci on both nucleoid and septum, and coordinates with FtsZ for the next cell division. Fl圜ut ® NotI is expressed and purified from E.coli that carries the recombinant NotI gene. The compact packaging of the deinococcal genome and cell membrane formation is hindered in ftsK mutants. The absence of drFtsK causes many defects in morphology at both cellular and nucleoid levels. radiodurans R1 (drFtsK) for the first time and showed it to be an active protein. Filament temperature-sensitive mutant K (FtsK), a multifunctional protein, helps in pumping the septum-trapped DNA in several bacteria. Very little is known about how the tightly packed genome is accurately segregated and the next divisional plane is determined. It is polyploid and harbors a multipartite genome comprised of 2 chromosomes and 2 plasmids, packaged in a doughnut-shaped toroidal nucleoid. IMPORTANCE Deinococcus radiodurans show extraordinary resistance to gamma radiation. These results suggest that FtsK forms a part of chromosome segregation, cell envelope, and cell division machinery in D. Nearly, similar positional dynamicity of FtsK was observed in cells recovering from gamma radiation exposure. The alignment of its foci shifts from old to new septum indicating its cellular dynamics with the FtsZ ring during the cell division process. drFtsK coordinates its movement with nucleoid separation. In vivo localization studies of drFtsK-RFP show that it forms multiple foci on nucleoid as well as on the membrane with maximum density on the septum. Microscopic examination of different domain deletion mutants of this protein reveals alterations in cellular membrane architecture and nucleoid morphology. ![]() Enjoy the enhanced performance and added value of our engineered enzymes at the same. drFtsK interacts with various cell division and genome segregation proteins of D. All HF-restriction enzymes come with Gel Loading Dye, Purple (6X). It stimulates the site-specific recombination catalyzed by Escherichia coli tyrosine recombi-nases. drFtsK shows the activity characteristics of a typical FtsK/SpoIIIE/Tra family. In this study, for the first time, we report the characterization of FtsK from the radioresistant MGH bacterium Deinococcus radiodur-ans R1 (drFtsK). Only limited reports, however, are available on the interdependent regulation of genome segregation and cell division in multipartite genome harboring (MGH) bacteria. Most of the studies in single chromosome-containing bacteria have established the role of FtsK in chromosome dimer resolution (CDR), connecting the bacterial chromosome segregation process with cell division. Filament temperature-sensitive mutant K (FtsK)/SpoIIIE family proteins are DNA translocases known as the fastest DNA motor proteins that use ATP for their movement on DNA.
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