Linked Life Data

9930652

Source:http://linkedlifedata.com/resource/pubmed/id/9930652

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-4-13
pubmed:abstractText
Despite extensive knowledge of the in vitro polymerization properties of nuclear lamins, it is still not well understood how the nuclear lamina assembles in vivo. To learn more about the relationship between in vitro and in vivo polymerization of nuclear lamins, we expressed Drosophila lamin Dm0, mutant proteins, having well defined alterations of their in vitro polymerization properties, in Sf9 cells using the baculovirus system. All lamin Dm0 mutants assembled into fibrillar aggregates indistinguishable in morphology from those assembled by the wild-type protein. However, in contrast to wild-type lamin Dm0, mutant proteins were extracted with buffers of physiological ionic strength and pH containing Triton X-100. These results indicate that various types of lamin dimer-dimer interactions can be disrupted without affecting the morphology of the lamin Dm0 polymer. However, all types of dimer-dimer interactions tested appear to be important for full polymer stability. In addition, we analyzed the polymer formation of two Drosophila lamin C mutants and found that a segment in the carboxy-terminal tail domain is required for assembly of lamin C paracrystals at the nuclear lamina.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0171-9335
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
276-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Assembly of Drosophila lamin Dm0 and C mutant proteins studied with the baculovirus system.
pubmed:affiliation
Division of Electron Microscopy, Biocenter of the University of Würzburg, Germany. krohne@biozentrum.uni-wuerzburg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't