Relocalization of an 82-kDa protein from lampbrush loops into the nucleoskeleton during amphibian oogenesis

Affinity-purified antibodies directed against an 82-kDa oocyte nuclear protein ofPleurodeles waltl (Amphibia, Urodela) were prepared using antigen bound to nitrocellulose paper. The specificity of the antibody was controlled on two-dimensional electrophoretic gels of nuclear proteins. The intranuclear distribution of the 82-kDa protein was analyzed by the indirect immunofluorescence method on spreads of oocyte nuclear content. Localization of the protein appeared to be extremely variable. The antibody recognized the protein (a) on normal and landmark loop matrices (but not simultaneously), (b) on ribonucleoprotein particles associated (or not) with the nucleoskeleton and (c) on nucleoli. This suggests the intervention of the protein at a certain physiological moment in the transcriptional or posttranscriptional process.