scholarly journals Nucleolar protein B23 has molecular chaperone activities

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pp. 905-912 ◽  
Author(s):  
Attila Szebeni ◽  
Mark O.J. Olson
2003 ◽  
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pp. 9107-9115 ◽  
Author(s):  
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Kamini Hingorani ◽  
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Mark O. J. Olson

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Mark O.J. Olson

2004 ◽  
Vol 280 (7) ◽  
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Author(s):  
Nian Huang ◽  
Sandeep Negi ◽  
Attila Szebeni ◽  
Mark O. J. Olson

Biochemistry ◽  
1997 ◽  
Vol 36 (13) ◽  
pp. 3941-3949 ◽  
Author(s):  
Attila Szebeni ◽  
Bam Mehrotra ◽  
Amy Baumann ◽  
Stephen A. Adam ◽  
Paul T. Wingfield ◽  
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1994 ◽  
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T. Takahashi ◽  
S. Yoshida ◽  
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2006 ◽  
Vol 50 (3) ◽  
pp. 225-234 ◽  
Author(s):  
Yoshimi Tsuda ◽  
Yoshio Mori ◽  
Takayuki Abe ◽  
Tetsuo Yamashita ◽  
Toru Okamoto ◽  
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eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Daniel G Booth ◽  
Masatoshi Takagi ◽  
Luis Sanchez-Pulido ◽  
Elizabeth Petfalski ◽  
Giulia Vargiu ◽  
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When the nucleolus disassembles during open mitosis, many nucleolar proteins and RNAs associate with chromosomes, establishing a perichromosomal compartment coating the chromosome periphery. At present nothing is known about the function of this poorly characterised compartment. In this study, we report that the nucleolar protein Ki-67 is required for the assembly of the perichromosomal compartment in human cells. Ki-67 is a cell-cycle regulated protein phosphatase 1-binding protein that is involved in phospho-regulation of the nucleolar protein B23/nucleophosmin. Following siRNA depletion of Ki-67, NIFK, B23, nucleolin, and four novel chromosome periphery proteins all fail to associate with the periphery of human chromosomes. Correlative light and electron microscopy (CLEM) images suggest a near-complete loss of the entire perichromosomal compartment. Mitotic chromosome condensation and intrinsic structure appear normal in the absence of the perichromosomal compartment but significant differences in nucleolar reassembly and nuclear organisation are observed in post-mitotic cells.


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