Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-3-1
pubmed:abstractText
The yeast mitochondrial protein Suv3p is a putative NTP-dependent RNA helicase. Here we report that in cells lacking Suv3p, there is an approximately 50-fold increase in the excised form of the group I intron omega of the mitochondrial 31S rRNA gene. Surprisingly, little mature 21S rRNA accumulates in those cells; instead, unligated 21S rRNA exons appear. Intron overaccumulation could lead to spliced exon reopening via a reaction known to be catalyzed by group I introns in vitro. We also show that Suv3p is a functional component of a novel mitochondrial NTP-dependent 3'-to-5' exoribonuclease activity that can degrade group I intron RNAs. These findings account for group I intron overaccumulation in cells lacking Suv3p and define a novel function for putative RNA helicases in direct RNA degradation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal, http://linkedlifedata.com/resource/pubmed/chemical/Exoribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, http://linkedlifedata.com/resource/pubmed/chemical/RNA, mitochondrial, http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/RNA Nucleotidyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SUV3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
199-209
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8565066-Base Sequence, pubmed-meshheading:8565066-DEAD-box RNA Helicases, pubmed-meshheading:8565066-DNA, Fungal, pubmed-meshheading:8565066-Exons, pubmed-meshheading:8565066-Exoribonucleases, pubmed-meshheading:8565066-Fungal Proteins, pubmed-meshheading:8565066-Introns, pubmed-meshheading:8565066-Mitochondria, pubmed-meshheading:8565066-Molecular Sequence Data, pubmed-meshheading:8565066-RNA, pubmed-meshheading:8565066-RNA, Fungal, pubmed-meshheading:8565066-RNA, Ribosomal, pubmed-meshheading:8565066-RNA Helicases, pubmed-meshheading:8565066-RNA Nucleotidyltransferases, pubmed-meshheading:8565066-RNA Splicing, pubmed-meshheading:8565066-Recombinant Fusion Proteins, pubmed-meshheading:8565066-Saccharomyces cerevisiae, pubmed-meshheading:8565066-Saccharomyces cerevisiae Proteins
pubmed:year
1996
pubmed:articleTitle
The DExH box protein Suv3p is a component of a yeast mitochondrial 3'-to-5' exoribonuclease that suppresses group I intron toxicity.
pubmed:affiliation
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't