Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2000-1-13
pubmed:abstractText
RNAI is a short RNA, 108 nt in length, which regulates the replication of the plasmid ColE1. RNAI turns over rapidly, enabling plasmid replication rate to respond quickly to changes in plasmid copy number. Because RNAI is produced in abundance, is easily extracted and turns over quickly, it has been used as a model for mRNA in studying RNA decay pathways. The enzymes polynucleotide phosphorylase, poly(A) polymerase and RNase E have been demonstrated to have roles in both messenger and RNAI decay; it is reported here that these enzymes can work independently of one another to facilitate RNAI decay. The roles in RNAI decay of two further enzymes which facilitate mRNA decay, the exonuclease RNase II and the endonuclease RNase III, are also examined. RNase II does not appear to accelerate RNAI decay but it is found that, in the absence of RNase III, polyadenylated RNAI, unprocessed by RNase E, accumulates. It is also shown that RNase III can cut RNAI near nt 82 or 98 in vitro. An RNAI fragment corresponding to the longer of these can be found in extracts of an mc+ pcnB strain (which produces RNase III) but not of an rnc pcnB strain, suggesting that RNAI may be a substrate for RNase III in vivo. A possible pathway for the early steps in RNAI decay which incorporates this information is suggested.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/100RNP-polynucleotide phosphorylase, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Exoribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Polynucleotide Adenylyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Antisense, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering, http://linkedlifedata.com/resource/pubmed/chemical/ROM protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease III, http://linkedlifedata.com/resource/pubmed/chemical/pcnB protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease E, http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease III, E coli
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
145 ( Pt 11)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3089-100
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10589716-Bacterial Proteins, pubmed-meshheading:10589716-Blotting, Northern, pubmed-meshheading:10589716-DNA Replication, pubmed-meshheading:10589716-Endoribonucleases, pubmed-meshheading:10589716-Escherichia coli, pubmed-meshheading:10589716-Escherichia coli Proteins, pubmed-meshheading:10589716-Exoribonucleases, pubmed-meshheading:10589716-Mutation, pubmed-meshheading:10589716-Plasmids, pubmed-meshheading:10589716-Polymerase Chain Reaction, pubmed-meshheading:10589716-Polynucleotide Adenylyltransferase, pubmed-meshheading:10589716-Protein Processing, Post-Translational, pubmed-meshheading:10589716-RNA, Antisense, pubmed-meshheading:10589716-RNA, Bacterial, pubmed-meshheading:10589716-RNA, Messenger, pubmed-meshheading:10589716-RNA, Small Interfering, pubmed-meshheading:10589716-Ribonuclease III
pubmed:year
1999
pubmed:articleTitle
Absence of RNASE III alters the pathway by which RNAI, the antisense inhibitor of ColE1 replication, decays.
pubmed:affiliation
Institute of Cell and Molecular Biology, University of Edinburgh, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't