Linked Life Data

8488725

Source:http://linkedlifedata.com/resource/pubmed/id/8488725

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-6-9
pubmed:abstractText
In the yeast Saccharomyces cerevisiae, the nucleus undergoes dramatic shape changes during mitosis and mating. We have studied nuclear envelope dynamics during the processes of mitosis and conjugation using nuclear pore complexes as a marker for the nuclear envelope in wild-type cells and several cell-division-cycle (cdc) mutants. Three monoclonal antibodies are described that recognize nuclear pore complex-related antigens in S. cerevisiae. One of these antibodies, RL1, has been extensively characterized by Gerace and colleagues and recognizes nuclear pore complexes in mammalian and amphibian cells. By indirect immunofluorescence of yeast cells, all three antibodies yield a discontinuous nuclear rim stain. All three react with multiple nuclear-enriched proteins in immunoblots, including the nucleoporin protein encoded by the NSP1 gene. When the antibodies were used in immunofluorescence experiments on mating cells, the nuclear pore complex staining pattern proved to be a sensitive indicator of nuclear fusion. Nuclei with closely apposed spindle pole bodies and unfused nuclear envelopes could be readily distinguished. Marked shape changes were observed in nuclei during fusion and segregation of the diploid nucleus into the zygotic bud. In cdc14 and cdc15 mutants that arrest late in mitosis, the elongated nuclear envelope extension that stretches between daughter nuclei during telophase was preserved. In cytokinesis-defective mutants (cdc3, cdc10, cdc11 and cdc12), the elongated nuclear envelope was usually resolved into two daughter nuclei in the absence of cytokinesis. These results indicate that nuclear envelope division is mechanically distinguishable from chromosome segregation, nucleolar segregation and cytokinesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0749-503X
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:geneSymbol
NSP1, cdc14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
235-49
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8488725-Amino Acid Sequence, pubmed-meshheading:8488725-Antibodies, Fungal, pubmed-meshheading:8488725-Antibody Specificity, pubmed-meshheading:8488725-Antigens, Fungal, pubmed-meshheading:8488725-Calcium-Binding Proteins, pubmed-meshheading:8488725-Cell Cycle, pubmed-meshheading:8488725-Cell Division, pubmed-meshheading:8488725-Conjugation, Genetic, pubmed-meshheading:8488725-Fluorescent Antibody Technique, pubmed-meshheading:8488725-Fungal Proteins, pubmed-meshheading:8488725-Microscopy, Fluorescence, pubmed-meshheading:8488725-Molecular Sequence Data, pubmed-meshheading:8488725-Nuclear Envelope, pubmed-meshheading:8488725-Nuclear Pore Complex Proteins, pubmed-meshheading:8488725-Nuclear Proteins, pubmed-meshheading:8488725-Saccharomyces cerevisiae, pubmed-meshheading:8488725-Saccharomyces cerevisiae Proteins, pubmed-meshheading:8488725-Telophase
pubmed:year
1993
pubmed:articleTitle
Nuclear pore complex antigens delineate nuclear envelope dynamics in vegetative and conjugating Saccharomyces cerevisiae.
pubmed:affiliation
Department of Biology, Yale University, New Haven, CT 06511-8112.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't