Identification and Characterization of Perinucleolar Compartment-Associated Protein

Abstract

During transformation, ribosome biogenesis increases concurrently with the size and number of nucleoli. The U3 snoRNP is involved in the cleavage of pre-rRNA and 4OS preribosomal particle assembly and contains a number of proteins, including Sof1 and fibrillarin, whose roles in the complex are unclear. Depletion of yeast Sof1 inhibits pre-rRNA processing, consistent with a functional role in the U3 snoRNP. Our research focuses on characterizing the role of human Sof1 (hSof1) in ribosome biogenesis by examining its localization and dynamics in live cells and its interactions. hSof1, like fibrillarin, localizes to both the nucleolus and nucleoplasm. However, unlike fibrillarin, hSof1 is also in the granular component of nucleoli and responds differently to the inhibition of the transcription of pre- rRNA. In addition, hSof1 -GFP also exhibits a higher nuclear mobility than fibrillarin-GFP and is a nucleocytoplasmic shuttling protein.

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Document Details

Document Type
Technical Report
Publication Date
Sep 01, 2002
Accession Number
ADA410865

Entities

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  • Daniel J. Leary
  • Sui Huang

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  • Northwestern University

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  • Abstracts
  • Biogenesis
  • Biology
  • Biomedical Research
  • Carrier Proteins
  • Cell Biology
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  • Biology

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