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Proteomic and targeted analytical identification of BXDC1 and EBNA1BP2 as dynamic scaffold proteins in the nucleolus
Author(s) -
Hirano Yasuhiro,
Ishii Kohei,
Kumeta Masahiro,
Furukawa Kazuhiro,
Takeyasu Kunio,
Horigome Tsuneyoshi
Publication year - 2009
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2008.01262.x
Subject(s) - biology , identification (biology) , computational biology , nucleolus , scaffold , proteomics , scaffold protein , microbiology and biotechnology , genetics , engineering , signal transduction , ecology , gene , cytoplasm , biomedical engineering
The nuclear matrix has classically been assumed to be a solid structure coherently aligning nuclear components, but its real nature remains obscure. We separated the proteins in a ribonucleoprotein‐containing nuclear matrix fraction of HeLa cells by reversed‐phase HPLC followed by SDS‐PAGE, and identified 83 proteins through peptide mass fingerprint (PMF) analysis. Many nucleolar proteins, classical nuclear matrix proteins, RNA binding proteins, cytoskeletal proteins and five uncharacterized proteins were identified in this fraction. Four of the latter proteins were localized to the cell nucleus, BXDC1 and EBNA1BP2 being especially localized to the nucleolus. Fluorescence recovery after photobleaching and RNAi knockdown analyses suggested that BXDC1 and EBNA1BP2 function in a dynamic scaffold for ribosome biogenesis.