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Vol. 12, Issue 11, 3502-3514, November 2001
Istituto di Genetica Biochimica ed Evoluzionistica del Consiglio
Nazionale delle Richerche, Pavia 27100, Italy
Heterogeneous nuclear ribonucleoprotein (hnRNP) HAP (hnRNP A1
interacting protein) is a multifunctional protein with roles in RNA
metabolism, transcription, and nuclear structure. After stress
treatments, HAP is recruited to a small number of nuclear bodies,
usually adjacent to the nucleoli, which consist of clusters of
perichromatin granules and are depots of transcripts synthesized before
stress. In this article we show that HAP bodies are sites of
accumulation for a subset of RNA processing factors and are related to
Sam68 nuclear bodies (SNBs) detectable in unstressed cells. Indeed, HAP
and Sam68 are both present in SNBs and in HAP bodies, that we rename
"stress-induced SNBs." The determinants required for the
redistribution of HAP lie between residue 580 and 788. Different
portions of this region direct the recruitment of the green fluorescent
protein to stress-induced SNBs, suggesting an interaction of HAP with
different components of the bodies. With the use of the 580-725 region
as bait in a two-hybrid screening, we have selected SRp30c and 9G8, two
members of the SR family of splicing factors. Splicing factors are
differentially affected by heat shock: SRp30c and SF2/ASF are
efficiently recruited to stress-induced SNBs, whereas the distribution
of SC35 is not perturbed. We propose that the differential
sequestration of splicing factors could affect processing of specific
transcripts. Accordingly, the formation of stress-induced SNBs is
accompanied by a change in the splicing pattern of the adenovirus E1A transcripts.
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