rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1993-11-19
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pubmed:databankReference |
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pubmed:abstractText |
The NgoII restriction-modification (R-M) system of Neisseria gonorrhoeae recognizes the sequence 5'-GGCC-3'. This system is encoded by two separate genes, dcmB for the methyltransferase (MTase) and dcrB for the restriction endonuclease (ENase). Three strains that vary in their NgoII phenotype were examined. Strain Pgh3-2 produced detectable levels of both enzymes, strain F62 lacked detectable levels of the dcrB gene product, and strain WR302 failed to produce either gene product. Strains that lacked either enzyme activity still possessed the genes that encode them. Transcriptional fusions of dcrB in strains F62 and Pgh3-2 indicate that this gene is transcribed at nearly identical levels in each strain. The DNA encoding the NgoII R-M system was cloned from the three strains, and the nucleotide sequence was determined. The dcrB genes of WR302 and F62 possess the same frameshift mutation (base position 1435) which would result in a truncated protein. The WR302 dcmB was found to have a point mutation that changed Arg288 (a residue that is conserved in all prokaryotic and phage cytosine MTases sequenced to date) to Trp.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Catechol 2,3-Dioxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Restriction-Modification Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Cytosine Methylases,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleases, Type II...,
http://linkedlifedata.com/resource/pubmed/chemical/Dioxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/GGCC-specific DNA methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/GGCC-specific type II...,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0378-1119
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
132
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pubmed:geneSymbol |
dcmB,
dcrB,
ngoII,
xylE
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15-20
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8406039-Amino Acid Sequence,
pubmed-meshheading:8406039-Base Sequence,
pubmed-meshheading:8406039-Catechol 2,3-Dioxygenase,
pubmed-meshheading:8406039-DNA, Bacterial,
pubmed-meshheading:8406039-DNA Restriction-Modification Enzymes,
pubmed-meshheading:8406039-DNA-Cytosine Methylases,
pubmed-meshheading:8406039-Deoxyribonucleases, Type II Site-Specific,
pubmed-meshheading:8406039-Dioxygenases,
pubmed-meshheading:8406039-Frameshift Mutation,
pubmed-meshheading:8406039-Genetic Variation,
pubmed-meshheading:8406039-Molecular Sequence Data,
pubmed-meshheading:8406039-Neisseria gonorrhoeae,
pubmed-meshheading:8406039-Oxygenases,
pubmed-meshheading:8406039-Recombinant Fusion Proteins,
pubmed-meshheading:8406039-Restriction Mapping,
pubmed-meshheading:8406039-Sequence Homology, Amino Acid,
pubmed-meshheading:8406039-Transcription, Genetic
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pubmed:year |
1993
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pubmed:articleTitle |
Natural variation of the NgoII restriction-modification system of Neisseria gonorrhoeae.
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pubmed:affiliation |
Department of Microbiology, University of Maryland, College Park 20742.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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