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Aggregation of Ribosomal Protein S6 at Nucleolus Is Cell Cycle‐Controlled and Its Function in Pre‐rRNA Processing Is Phosphorylation Dependent
Author(s) -
Zhang Duo,
Chen HuiPeng,
Duan HaiFeng,
Gao LiHua,
Shao Yong,
Chen KeYan,
Wang YouLiang,
Lan FengHua,
Hu XianWen
Publication year - 2016
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.25458
Subject(s) - nucleolus , eukaryotic small ribosomal subunit , ribosomal protein , ribosomal rna , ribosomal protein s6 , protein subunit , phosphorylation , biology , ribosomal dna , microbiology and biotechnology , eukaryotic large ribosomal subunit , 18s ribosomal rna , ribosome , nucleus , genetics , rna , protein phosphorylation , gene , protein kinase a , phylogenetics
Ribosomal protein S6 (rpS6) has long been regarded as one of the primary r‐proteins that functions in the early stage of 40S subunit assembly, but its actual role is still obscure. The correct forming of 18S rRNA is a key step in the nuclear synthesis of 40S subunit. In this study, we demonstrate that rpS6 participates in the processing of 30S pre‐rRNA to 18S rRNA only when its C‐terminal five serines are phosphorylated, however, the process of entering the nucleus and then targeting the nucleolus does not dependent its phosphorylation. Remarkably, we also find that the aggregation of rpS6 at the nucleolus correlates to the phasing of cell cycle, beginning to concentrate in the nucleolus at later S phase and disaggregate at M phase. J. Cell. Biochem. 117: 1649–1657, 2016. © 2015 Wiley Periodicals, Inc.