Relevant bibliographies by topics / HpyAII Endonuclease

Academic literature on the topic 'HpyAII Endonuclease'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "HpyAII Endonuclease"

1

Ando, T., R. A. Aras, K. Kusugami, M. J. Blaser, and T. M. Wassenaar. "Evolutionary History of hrgA, Which Replaces the Restriction Gene hpyIIIR in the hpyIII Locus of Helicobacter pylori." Journal of Bacteriology 185, no. 1 (January 1, 2003): 295–301. http://dx.doi.org/10.1128/jb.185.1.295-301.2003.

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ABSTRACT A recently identified Helicobacter pylori gene, hrgA, was previously reported to be present in 70 (33%) of 208 strains examined (T. Ando, T. M. Wassenaar, R. M. Peek, R. A. Aras, A. I. Tschumi, L.-J. Van Doorn, K. Kusugami, and M. J. Blaser, Cancer Res. 62:2385-2389, 2002). Sequence analysis of nine such strains indicated that in each strain hrgA replaced hpyIIIR, which encodes a restriction endonuclease and which, together with the gene for its cognate methyltransferase, constitutes the hpyIII locus. As a consequence of either the hrgA insertion or independent mutations, hpyIIIM function was lost in 11 (5%) of the 208 strains examined, rendering chromosomal DNA sensitive to MboI digestion. The evolutionary history of the locus containing either hpyIII or hrgA was reconstructed. By homologous recombination involving flanking sequences, hrgA and hpyIIIR can replace one another in the hpyIII locus, and there is simultaneous replacement of several flanking genes. These findings, combined with the hpyIM/iceA2 locus discovered previously, suggest that the two most strongly conserved methylase genes of H. pylori, hpyIIIM and hpyIM, are both preceded by alternative genes that compete for presence at their loci.
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2

Chan, Siu-Hong, Lars Opitz, Lauren Higgins, Diana O'loane, and Shuang-yong Xu. "Cofactor Requirement of HpyAV Restriction Endonuclease." PLoS ONE 5, no. 2 (February 5, 2010): e9071. http://dx.doi.org/10.1371/journal.pone.0009071.

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3

Czapinska, Honorata, Monika Sokolowska, and Matthias Bochtler. "ββα-Me restriction endonuclease Hpy99I in complex with target DNA." Acta Crystallographica Section A Foundations of Crystallography 65, a1 (August 16, 2009): s131—s132. http://dx.doi.org/10.1107/s0108767309097396.

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4

Sokolowska, Monika, Honorata Czapinska, and Matthias Bochtler. "Crystal structure of the ββα-Me type II restriction endonuclease Hpy99I with target DNA." Nucleic Acids Research 37, no. 11 (April 20, 2009): 3799–810. http://dx.doi.org/10.1093/nar/gkp228.

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5

Tabar, Elham Atefi, Hamid Staji, and Ali Mahdavi. "Comparative restriction enzyme mapping of Campylobacter jejuni isolates from turkeys and broilers based on flaA flagellar gene using HpyF3I endonuclease." Folia Microbiologica 64, no. 2 (August 27, 2018): 189–95. http://dx.doi.org/10.1007/s12223-018-0643-y.

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6

Humbert, Olivier, and Nina R. Salama. "The Helicobacter pylori HpyAXII restriction–modification system limits exogenous DNA uptake by targeting GTAC sites but shows asymmetric conservation of the DNA methyltransferase and restriction endonuclease components." Nucleic Acids Research 36, no. 21 (October 31, 2008): 6893–906. http://dx.doi.org/10.1093/nar/gkn718.

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7

Kumar, Sumith, Sushant Bangru, Ritesh Kumar, and Desirazu N. Rao. "Promiscuous DNA cleavage by HpyAII endonuclease is modulated by the HNH catalytic residues." Bioscience Reports 40, no. 9 (September 2020). http://dx.doi.org/10.1042/bsr20201633.

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Abstract Helicobacter pylori is a carcinogenic bacterium that is responsible for 5.5% of all human gastric cancers. H. pylori codes for an unusually large number of restriction–modification (R–M) systems and several of them are strain-specific and phase-variable. HpyAII is a novel Type IIs phase-variable restriction endonuclease present in 26695 strain of H. pylori. We show that HpyAII prefers two-site substrates over one-site substrates for maximal cleavage activity. HpyAII is less stringent in metal ion requirement and shows higher cleavage activity with Ni2+ over Mg2+. Mutational analysis of the putative residues of the HNH motif of HpyAII confirms that the protein has an active HNH site for the cleavage of DNA. However, mutation of the first Histidine residue of the HNH motif to Alanine does not abolish the enzymatic activity, but instead causes loss of fidelity compared with wildtype HpyAII. Previous studies have shown that mutation of the first Histidine residue of the HNH motif of all other known HNH motif motif-containing enzymes completely abolishes enzymatic activity. We found, in the case of HpyAII, mutation of an active site residue leads to the loss of endonuclease fidelity. The present study provides further insights into the evolution of restriction enzymes.
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8

Miyazono, Ken-ichi, Delong Wang, Tomoko Ito, and Masaru Tanokura. "Crystal structure and DNA cleavage mechanism of the restriction DNA glycosylase R.CcoLI from Campylobacter coli." Scientific Reports 11, no. 1 (January 13, 2021). http://dx.doi.org/10.1038/s41598-020-79537-y.

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AbstractWhile most restriction enzymes catalyze the hydrolysis of phosphodiester bonds at specific nucleotide sequences in DNA, restriction enzymes of the HALFPIPE superfamily cleave N-glycosidic bonds, similar to DNA glycosylases. Apurinic/apyrimidinic (AP) sites generated by HALFPIPE superfamily proteins are cleaved by their inherent AP lyase activities, other AP endonuclease activities or heat-promoted β-elimination. Although the HALFPIPE superfamily protein R.PabI, obtained from a hyperthermophilic archaea, Pyrococcus abyssi, shows weak AP lyase activity, HALFPIPE superfamily proteins in mesophiles, such as R.CcoLI from Campylobacter coli and R. HpyAXII from Helicobacter pylori, show significant AP lyase activities. To identify the structural basis for the AP lyase activity of R.CcoLI, we determined the structure of R.CcoLI by X-ray crystallography. The structure of R.CcoLI, obtained at 2.35-Å resolution, shows that a conserved lysine residue (Lys71), which is stabilized by a characteristic β-sheet structure of R.CcoLI, protrudes into the active site. The results of mutational assays indicate that Lys71 is important for the AP lyase activity of R.CcoLI. Our results help to elucidate the mechanism by which HALFPIPE superfamily proteins from mesophiles efficiently introduce double-strand breaks to specific sites on double-stranded DNA.
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