Structures and dynamics of Drosophila Tpr inconsistent with a static, filamentous structure.

Here we report immunofluorescence localizations of the Drosophila Tpr protein which are inconsistent with a filament-forming protein statically associated with nuclear pore complex-associated intranuclear filaments. Using tissues from throughout the Drosophila life cycle, we observe that Tpr is often localized to discontinuous, likely granular or particulate structures in the deep nuclear interior. These apparent granules have no obvious connectivity to pore complexes in the nuclear periphery, and are often localized on the surfaces of chromosomes and to the perinucleolar region. Most strikingly, after 1 h of heat shock, the great majority of the Tpr in the deep nuclear interior accumulates at a single heat shock puff, while Tpr in the nuclear periphery appears unchanged. This heat shock puff, 93D, is a known repository for many components of pre-mRNA metabolism during heat shock. Although we do not observe Tpr at sites of transcription under normal conditions, the 93D heat shock result leads us to favor a role for Tpr in mRNA metabolism, such as the transport of mRNA through the nuclear interior to nuclear pore complexes. Consistent with this, we observe networks of Tpr containing granules spanning between the nucleolus and the nuclear periphery which are also decorated by an anti-SR protein antibody. Since we also observe Drosophila Tpr in reticular or fibrous structures in other nuclei, such as salivary gland polytene nuclei, these results indicate that Tpr can exist in at least two structural forms, and suggest that Tpr may relocalize or even change structural forms in response to cellular needs. (c) 2002 Elsevier Science (USA).