Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1993-3-16
pubmed:databankReference
pubmed:abstractText
F1845, the fimbrial adhesin of a diarrhea-associated Escherichia coli, confers upon the bacteria the ability to adhere to cultured epithelial cells in a diffuse pattern. The fimbrial subunit gene, daaE, is encoded on a polycistronic mRNA which is processed endoribonucleolytically to produce a stable message encoding only daaE. The processing event occurs in bacterial strains with mutations in RNase III or RNase E, the only endoribonucleases which have been implicated in the processing of E. coli mRNA. Sequences encoding a stem-loop structure downstream of daaE play an essential role in determining the stability of the daaE mRNA. Rapid degradation of the sequences upstream of the cleavage site occurs upon processing, suggesting that processing of the F1845 polycistronic mRNA results in differential expression of genes involved in the biogenesis of fimbriae.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-1670929, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-1708438, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-1713282, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-1846032, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-1943710, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-1967170, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-2449283, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-2568258, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-2568985, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-2583104, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-2860096, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-2882856, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-2902826, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-3061803, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-3072246, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-3148948, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-3308454, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-3881765, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-6234400, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-6237955, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-6295879, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-6310323, http://linkedlifedata.com/resource/pubmed/commentcorrection/8094558-6312838
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Escherichia coli, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease III, http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase, http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease E, http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease III, E coli
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
90
pubmed:geneSymbol
daaE
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1455-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:8094558-Adhesins, Escherichia coli, pubmed-meshheading:8094558-Amino Acid Sequence, pubmed-meshheading:8094558-Bacterial Outer Membrane Proteins, pubmed-meshheading:8094558-Base Sequence, pubmed-meshheading:8094558-Blotting, Northern, pubmed-meshheading:8094558-DNA, Bacterial, pubmed-meshheading:8094558-Endoribonucleases, pubmed-meshheading:8094558-Escherichia coli, pubmed-meshheading:8094558-Escherichia coli Proteins, pubmed-meshheading:8094558-Gene Expression, pubmed-meshheading:8094558-Genes, Bacterial, pubmed-meshheading:8094558-Molecular Sequence Data, pubmed-meshheading:8094558-Mutagenesis, Site-Directed, pubmed-meshheading:8094558-Plasmids, pubmed-meshheading:8094558-RNA, Messenger, pubmed-meshheading:8094558-Recombinant Fusion Proteins, pubmed-meshheading:8094558-Ribonuclease III, pubmed-meshheading:8094558-Transcription, Genetic, pubmed-meshheading:8094558-beta-Galactosidase
pubmed:year
1993
pubmed:articleTitle
mRNA processing independent of RNase III and RNase E in the expression of the F1845 fimbrial adhesin of Escherichia coli.
pubmed:affiliation
Department of Microbiology, University of Washington, Seattle 98195.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.