Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.26.3 (RNase III)
 1,015 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ribonuclease III from Escherichia coli has been purified to apparent homogeneity by affinity chromatography on immobilized double-stranded RNA. Polyacrylamide gel electrophoresis of the purified enzyme in the presence of sodium dodecyl sulfate gave one band of protein with a molecular weight of approximately 25,000. Chromatography on Sephadex G-100 is consistent with a molecular weight of 50,000, suggesting that the native enzyme is a dimer. RNase III cuts some single-stranded RNAs, such as bacteriophage T7 early RNA, at specific sites in vivo. This RNA is cut as these same sites by the purified enzyme under all conditions tested. However, at low ionic strength relatively small increases in enzyme concentration produce cuts as secondary sites. At high ionic strength, the enzyme's preference for the sites cut in vivo is more pronounced and secondary cuts are made only at very high enzyme concentrations. Secondary cuts are shown to occur at specific sites and are made in a variety of RNAs even from sources other than E. coli. By cutting RNAs at secondary sites it should be possible to generate RNA fragments which would be useful in a number of studies.
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PMID:RNase III cleavage of single-stranded RNA. Effect of ionic strength on the fideltiy of cleavage. 93 8

Streptococcus mutans is the primary etiological agent of human dental caries. Its major virulence factors, glucosyltransferases (Gtfs), utilize sucrose to synthesize extracellular polysaccharides (EPS), leading to the formation of dental plaque biofilm. The current study was designed to develop a novel self-targeting gene editing technology that targeted gtfs to inhibit biofilms formation. The CRISPR-Cas system (ie, clustered regularly interspaced short palindromic repeat, with CRISPR-associated proteins) provides sequence-specific protection against foreign genetic materials in archaea and bacteria, and has been widely developed for genomic engineering. The first aim of this study was to test whether components of the CRISPR-Cas9 system from S mutans UA159 is necessary to defend against foreign DNA. The data showed that a suitable PAM site, tracrRNA, Cas9, and RNase III are indispensable elements to perform normal function of S mutans CRISPR-Cas9 system. Based on these results, we designed self-targeting CRISPR arrays (containing spacer sequences identifying with gtfB) and cloned them onto plasmids. Afterward, we transformed the plasmids and editing templates into UA159 (self-targeting) to acquire desired mutants. Our data showed that this technology performed well and was able to successfully edit gtfB or gtfBgtfC genes. This resulted in high reduction in EPS synthesis and was able to breakdown biofilm formation, which is also a promising tool for dental clinics in order to prevent the formation of S mutans biofilms in the future.
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PMID:Genome editing in Streptococcus mutans through self-targeting CRISPR arrays. 3032 21