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Giedrius Gasiunas Tomas Sinkunas Virginijus Siksnys 《Cellular and molecular life sciences : CMLS》2014,71(3):449-465
Bacteriophages (phages) infect bacteria in order to replicate and burst out of the host, killing the cell, when reproduction is completed. Thus, from a bacterial perspective, phages pose a persistent lethal threat to bacterial populations. Not surprisingly, bacteria evolved multiple defense barriers to interfere with nearly every step of phage life cycles. Phages respond to this selection pressure by counter-evolving their genomes to evade bacterial resistance. The antagonistic interaction between bacteria and rapidly diversifying viruses promotes the evolution and dissemination of bacteriophage-resistance mechanisms in bacteria. Recently, an adaptive microbial immune system, named clustered regularly interspaced short palindromic repeats (CRISPR) and which provides acquired immunity against viruses and plasmids, has been identified. Unlike the restriction–modification anti-phage barrier that subjects to cleavage any foreign DNA lacking a protective methyl-tag in the target site, the CRISPR–Cas systems are invader-specific, adaptive, and heritable. In this review, we focus on the molecular mechanisms of interference/immunity provided by different CRISPR–Cas systems. 相似文献
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Sokolowska M Kaus-Drobek M Czapinska H Tamulaitis G Siksnys V Bochtler M 《Cellular and molecular life sciences : CMLS》2007,64(18):2351-2357
It has long been known that most Type II restriction endonucleases share a conserved core fold and similar active-sites. The
same core folding motif is also present in the MutH protein, a component of the bacterial DNA mismatch repair machinery. In
contrast to most Type II restriction endonucleases, which assemble into functional dimers and catalyze double-strand breaks,
MutH is a monomer and nicks hemimethylated DNA. Recent biochemical and crystallographic studies demonstrate that the restriction
enzymes BcnI and MvaI share many additional features with MutH-like proteins, but not with most other restriction endonucleases.
The structurally similar monomers all recognize approximately symmetric target sequences asymmetrically. Differential sensitivities
to slight substrate asymmetries, which could be altered by protein engineering, determine whether the enzymes catalyze only
single-strand nicks or double-strand breaks.
M. Sokolowska, M. Kaus-Drobek: These authors contributed equally to this work.
Received 12 March 2007; received after revision 28 April 2007; accepted 3 May 2007 相似文献
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