Linked Life Data

10395901

Source:http://linkedlifedata.com/resource/pubmed/id/10395901

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-8-17
pubmed:abstractText
A tom1-1 mutant was isolated from Saccharomyces cerevisiae. At high temperatures, 60% of the cells were arrested as dumbbell forms with a single large nucleus containing duplicated DNA and a short spindle. Electron-microscopy showed electron-dense structures scattered within the nucleus. Indirect immunofluorescent microscopy revealed these structures to be fragmented nucleoli since the dotted structures were stained with anti-Nop1(fibrillarin) antibody in large regions of the nuclei. Fluorescent in situ hybridization analysis using oligo(dT) revealed nuclear accumulation of poly(A)+RNA. We cloned TOM1 which encodes a large protein (380kDa) with a hect (homologous to E6-AP C terminus)-domain at its C terminus. Deletions of either this hect-region or the entire gene made cellular growth temperature-sensitive. Site-directed mutagenesis of the conserved cysteine residue (tom1C3235A) in the hect-domain, supposed to be necessary for thioester-bond formation with ubiquitin, abolished the gene function. When a functional glutathione S-transferase (GST)-tagged hect protein was overproduced, it facilitated the protein conjugation with a myc-tagged ubiquitinRA, while this was not seen when GST-hectC3235A was overproduced. The protein conjugation with a hemagglutinin-tagged Smt3 was not affected by the overproduction of GST-hect. Taken together, we suggest that Tom1 is a ubiquitin ligase. As a multi-copy suppressor of tom1, we isolated STM3/NPI46/FPR3 which encodes a nucleolar nucleolin-like protein. We discuss possible functions of Tom1 with respect to the pleiotropic defects of nuclear division, maintenance of nuclear structure, and nucleocytoplasmic transport.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
234
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
285-95
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10395901-Amino Acid Sequence, pubmed-meshheading:10395901-Binding Sites, pubmed-meshheading:10395901-Biological Transport, pubmed-meshheading:10395901-Cell Division, pubmed-meshheading:10395901-Cell Nucleus, pubmed-meshheading:10395901-Cytoplasm, pubmed-meshheading:10395901-Fungal Proteins, pubmed-meshheading:10395901-G2 Phase, pubmed-meshheading:10395901-Gene Dosage, pubmed-meshheading:10395901-Gene Expression Regulation, pubmed-meshheading:10395901-Homeodomain Proteins, pubmed-meshheading:10395901-Ligases, pubmed-meshheading:10395901-Mitosis, pubmed-meshheading:10395901-Mutation, pubmed-meshheading:10395901-Peptidylprolyl Isomerase, pubmed-meshheading:10395901-RNA, Messenger, pubmed-meshheading:10395901-Recombinant Fusion Proteins, pubmed-meshheading:10395901-Saccharomyces cerevisiae, pubmed-meshheading:10395901-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10395901-Sequence Homology, Amino Acid, pubmed-meshheading:10395901-Temperature, pubmed-meshheading:10395901-Ubiquitin-Protein Ligases, pubmed-meshheading:10395901-Ubiquitins
pubmed:year
1999
pubmed:articleTitle
Yeast tom1 mutant exhibits pleiotropic defects in nuclear division, maintenance of nuclear structure and nucleocytoplasmic transport at high temperatures.
pubmed:affiliation
Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't