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- W2184808212 abstract "A Drosophila cell-free system wasusedtocharacterize proteins thatarerequired for targeting vesicles tochromatin andforfusion ofvesicles toformnuclear envelopes. Treatment ofvesicles with1M NaClabolished their ability tobindtochromatin. Binding ofsalt-treated vesicles tochromatin could berestored byadding thedialyzed salt extract. LaminDm isoneoftheperipheral proteins whoseactivity wasrequired, since supplying interphase laminisoforms DmlandDM2totheassembly extract restored binding. As opposed tothefindings inXenopus, okadaic acidhadnoaffect onvesicle binding. Trypsin digestion ofthesalt-stripped vesicles eliminated their association withchromatin evenin thepresence ofthedialyzed salt extract. Oncevesicles attached tochromatin surface, fusion events tookplace that werefoundtobesensitive toguanosine 5'-[y-thio]triph osphate (GTPyS). These chromatin-attached vesicles contained lamin Dm andotefin butnot gp210. Thus, these results showthat inDrosophila there aretwopopulations ofnuclear vesicles. Thepopulation that interacts first withchromatin contains laminandotefin and requires bothperipheral andintegral membraneproteins, whereas fusion ofvesicles requires GTPaseactivity." @default.
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- W2184808212 date "1997-01-01" @default.
- W2184808212 modified "2023-09-27" @default.
- W2184808212 title "Nuclear MembraneVesicle Targeting toChromatin in aDrosophila EmbryoCell-Free System" @default.
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