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The bamHIC gene, controlling the BamHI restriction-modification (R-M) system can functionally be replaced by providing pvuIIC or smaIC in trans. C BamHI, the protein product encoded by bamHIC, has been purified and shown to bind a 345-bp DNA fragment within the BamHI R-M system.
CciNI, an isoschizomer of NotI, has been isolated from Curtobacterium citreum. The enzyme cleaves within the recognition sequence 5 -GC↓GGCCGC-3 as indicated by the arrow.
Several restriction-modification (R-M) systems have been identified in Lactococcus lactis. Most of the systems have been plasmid encoded and function as phage-resistance mechanisms. At least five different type-II R-M systems, LlaAI,Lla BI, LlaCI, LlaDI and LlaEI, were identified in isolates from a mixed Cheddar starter culture. LlaAI and LlaBI recognized the DNA sequences 5 -↓GATC-3 and 5 ...
EcoRI recognizes and cleaves DNA at GAATTC sites and is one of the best characterized sequence-specific restriction endonucleases (ENases). In previous studies, an EcoRI mutant, which exhibited relaxed substrate specificity and cleaved both canonical and EcoRI star sites, was isolated. This mutant enzyme has Tyr instead of His 114 . Here, we subjected residue 114 of the EcoRI ENase...
SacNI, an isoschizomer of the restriction endonuclease, BanII [Sugisaki et al., Nucleic Acids Res. 10 (1982) 5747-5752], has been isolated from Streptomyces achromogenes N-J-H. SacNI recognizes the palindromic sequence, 5 -GRGCY/C, and cleaves within the recognition sequence, generating a 3 protruding RGCY end (where R = A or G, and Y = C or G).
We have characterized a family of related restriction-modification (R-M) systems from the soil bacteriumHerpetosiphon giganteus (Hgi). A comparison of their genetic organization reveals two types of regulatory proteins, called controlling ORF C. While one of these small reading frames derived from RM HgiCI seems to be an enhancer of its own promoter, evidence is provided for a silencer function...
A type-I R-M system was identified in B. subtilis. The genes comprising the system have striking similarity to type-I R-M systems observed in Enterobacteriaceae.
DNA duplexes containing a monosubstituted pyrophosphate internucleotide group, instead of a phosphodiester bond, were used as cross-linking reagent for the affinity modification of the restriction endonucleases EcoRII and MvaI (R EcoRII and R MvaI). An active group was introduced into the enzyme's recognition site or between the recognition site and flanking sequence. The substrate properties...
The Bsp6I restriction and modification (R-M) system has been localized on the plasmid pXH13, naturally occurring in the Bacillus sp. strain RFL6. The genes coding for the Bsp6I R-M system, a Fnu4HI isoschizomer recognizing the sequence GCNGC, have been cloned in Escherichia coli by two steps. The nucleotide sequence of a 2126-bp region containing the genes for restriction endonuclease (ENase; bsp6IR)...
BstF5I, a new restriction endonuclease (ENase) from Bacillus stearothermophilus F5, has been discovered. This enzyme recognizes 5 -GGATG-3 and cleaves DNA, generating a 2-base 3 extension: 5 -GGATG NN -3 3 -CCTAC NN -5 BstF5I is an isoschizomer of FokI and seems to be evolutionarily close to other nonpalindromic-recognizing ENases from thermophilic bacilli.
The genes encoding a class-IIN restriction-modification (R-M) system (MamI, sequence specificity5 -GATnn nnATC-3 3 -CTAnn nnTAG-5 from Microbacterium ammoniaphilum have been cloned in Escherichia coli.The vector used for cloning was plasmid pUC18 modified by the inclusion of three MamI recognition sites. Recombinant clones containing the mamIM gene in its genomic context became fully methylated...
The Sth132I restriction endonuclease (R.Sth132I) was detected in Streptococcus thermophilus ST132 and purified to near homogeneity by heparin Sepharose CL-6B affinity chromatography. Fragments from Sth132I digestion of plasmid DNA were subcloned into pUC19 in Escherichia coli DH5α and sequenced. Sequence analysis of inserts and their ligation junction sites revealed that Sth132I is a novel class-IIS...
The I-PpoI endonuclease is encoded by a group I intron found in the slime mold Physarum polycephalum. To initiate homing of its encoding intron, I-PpoI catalyzes a specific double-stranded break within a 15-bp recognition site. The high substrate specificities of I-PpoI and other homing endonucleases make these enzymes valuable tools for genomic mapping and sequencing. Here, we report on the ability...
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