Identification and Characterization of a Perinucleolar Compartment-Associated Protein
Abstract
During transformation, ribosome synthesis increases concurrently with the size and number of nucleoli. U3 snoRNA-associated complexes are involved in the cleavage of pre-rRNA and 4OS preribosome assembly and contain a number of proteins whose roles in the complex are unclear. Our research focused on characterizing the functional roles of human U3 snoRNA-associated factors by examining their localization and dynamics in live cells. We found that these factors can be divided into subclasses based on their localization and dynamics and showed for the first time that U3 snoRNA-associated proteins shuttle between nucleoli and the nucleoplasm and between nuclei and the cytoplasm. These studies have led us to propose a model for the assembly and function of U3 snoRNA-associated complexes. We also carried out more extensive studies of the U3 snoRNA-associated protein Sof1 which defined the protein domains necessary and sufficient for its localization, characterized its interactions, and disrupted its function. These studies have indicated that Sof1 has characteristics that distinguish it from other U3 snoRNA-associated proteins. Overall, these experiments have clarified the roles of Sof1 and other U3 snoRNA-associated factors in ribosome synthesis and have contributed to our understanding of ribosome synthesis as a whole.
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 01, 2003
- Accession Number
- ADA420169
Entities
People
- Daniel J. Leary
- Sui Huang
Organizations
- Northwestern University