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Bcp1 is the nuclear chaperone of Rpl23 in Saccharomyces cerevisiae


Ting, Ya Han and Lu, Ting Jun and Johnson, Arlen W. and Shie, JingTing and Chen, Bo Ru and Subbiah, Suresh Kumar and Lo, Kai Yin (2017) Bcp1 is the nuclear chaperone of Rpl23 in Saccharomyces cerevisiae. Journal of Biological Chemistry, 292 (2). 585 - 596. ISSN 0021-9258; ESSN: 1083-351X


Eukaryotic ribosomes are composed of rRNAs and ribosomal proteins. Ribosomal proteins are translated in the cytoplasm and imported into the nucleus for assembly with the rRNAs. It has been shown that chaperones or karyopherins responsible for import can maintain the stability of ribosomal proteins by neutralizing unfavorable positive charges and thus facilitate their transports. Among 79 ribosomal proteins in yeast, only a few are identified with specific chaperones. Besides the classic role in maintaining protein stability, chaperones have additional roles in transport, chaperoning the assembly site, and dissociation of ribosomal proteins from karyopherins. Bcp1 has been shown to be necessary for the export of Mss4, a phosphatidylinositol 4-phosphate 5-kinase, and required for ribosome biogenesis. However, its specific function in ribosome biogenesis has not been described. Here, we show that Bcp1 dissociates Rpl23 from the karyopherins and associates with Rpl23 afterward. Loss of Bcp1 causes instability of Rpl23 and deficiency of 60S subunits. In summary, Bcp1 is a novel 60S biogenesis factor via chaperoning Rpl23 in the nucleus.

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Additional Metadata

Item Type: Article
Divisions: Faculty of Medicine and Health Science
Publisher: American Society for Biochemistry and Molecular Biology
Keywords: Chaperone; Phosphoinositide; Protein stability; Ribosome; Ribosome assembly
Depositing User: Nida Hidayati Ghazali
Date Deposited: 31 Jan 2019 02:34
Last Modified: 31 Jan 2019 02:34
URI: http://psasir.upm.edu.my/id/eprint/60989
Statistic Details: View Download Statistic

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