scholarly journals Gene disruption of ribosomal protein L5 (RPL5) decreased the sensitivity of CHO-K1 cells to uncoupler carbonylcyanide-3-chlorophenylhydrazone

2019 ◽  
Vol 13 (6) ◽  
pp. 306-313
Author(s):  
Makoto Araki ◽  
Takuya Ishibashi ◽  
Masahiro Munesue ◽  
Kazuaki Ohashi ◽  
Yoshitaka Nobukuni ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Gene Disruption ◽  
Ribosomal Protein L5

scholarly journals Molecular cloning and nucleotide sequence of cDNA specific for rat ribosomal protein L5

1987 ◽  
Vol 168 (1) ◽  
pp. 83-87 ◽  
Author(s):  
Satoru TAMURA ◽  
Yuh KUWANO ◽  
Tatsuo NAKAYAMA ◽  
Shoji TANAKA ◽  
Tatsuo TANAKA ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Ribosomal Protein ◽  
Molecular Cloning ◽  
Ribosomal Protein L5

scholarly journals Perturbation of 60 S Ribosomal Biogenesis Results in Ribosomal Protein L5- and L11-dependent p53 Activation

2010 ◽  
Vol 285 (33) ◽  
pp. 25812-25821 ◽  
Author(s):  
Xiao-Xin Sun ◽  
Yue-Gang Wang ◽  
Dimitris P. Xirodimas ◽  
Mu-Shui Dai
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Biogenesis ◽  
P53 Activation ◽  
Ribosomal Protein L5

Mutual Induced Fit Binding of Xenopus Ribosomal Protein L5 to 5S rRNA

2003 ◽  
Vol 330 (5) ◽  
pp. 979-992 ◽  
Author(s):  
Jonathan P. DiNitto ◽  
Paul W. Huber
Keyword(s):  
Ribosomal Protein ◽  
5S Rrna ◽  
Induced Fit ◽  
Ribosomal Protein L5

Developmental expression and 5S rRNA-binding activity of Xenopus laevis ribosomal protein L5

1989 ◽  
Vol 9 (12) ◽  
pp. 5281-5288
Author(s):  
W M Wormington
Keyword(s):  
Ribosomal Protein ◽  
Mammalian Cells ◽  
Ribosomal Proteins ◽  
5S Rrna ◽  
Yeast Cells ◽  
Developmental Expression ◽  
Rrna Synthesis ◽  
Ribosome Assembly ◽  
Subunit Assembly ◽  
Ribosomal Protein L5

Ribosomal protein L5 binds specifically to 5S rRNA to form a complex that is a precursor to 60S subunit assembly in vivo. Analyses in yeast cells, mammalian cells, and Xenopus embryos have shown that the accumulation of L5 is not coordinated with the expression of other ribosomal proteins. In this study, the primary structure and developmental expression of Xenopus ribosomal protein L5 were examined to determine the basis for its distinct regulation. These analyses showed that L5 expression could either coincide with 5S rRNA synthesis and ribosome assembly or be controlled independently of these events at different stages of Xenopus development. L5 synthesis during oogenesis was uncoupled from the accumulation of 5S rRNa but coincided with subunit assembly. In early embryos, the inefficient translation of L5 mRNA resulted in the accumulation of a stable L5-5S rRNA complex before ribosome assembly at later stages of development. Additional results demonstrated that L5 protein synthesized in vitro bound specifically to 5S rRNA.

scholarly journals p53-Dependent Apoptotic Effect of Puromycin via Binding of Ribosomal Protein L5 and L11 to MDM2 and its Combination Effect with RITA or Doxorubicin

Cancers ◽  
2019 ◽  
Vol 11 (4) ◽  
pp. 582 ◽  
Author(s):  
Jung ◽  
Lee ◽  
Kim ◽  
Sim ◽  
Ahn ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Cancer Cells ◽  
Ribosomal Proteins ◽  
Antitumor Effect ◽  
Wild Type ◽  
Diphenyltetrazolium Bromide ◽  
Apoptotic Effect ◽  
Ribosomal Protein L5 ◽  
Proliferation Assays ◽  
Hct116 Cells

Among ribosomal proteins essential for protein synthesis, the functions of ribosomal protein L5 (RPL5) and RPL11 still remain unclear to date. Here, the roles of RPL5 and RPL11 were investigated in association with p53/p21 signaling in the antitumor effect of puromycin mainly in HCT116 and H1299 cancer cells. Cell proliferation assays using 3-[4,5-dimethylthiazole-2-yl]-2,5-diphenyltetrazolium bromide (MTT) assays and colony formation assays, cell cycle analysis, Reverse transcription polymerase chain reaction (RT-PCR) and Western blotting were performed in cancer cells. Puromycin exerted cytotoxic and anti-proliferative effects in p53 wild-type HCT116 more than in p53 null H1299 cells. Consistently, puromycin increased sub-G1, cleaved Poly (ADP-ribose) polymerase (PARP), activated p53, p21, and Mouse double minute 2 homolog (MDM2), and attenuated expression of c-Myc in HCT116 cells. Notably, puromycin upregulated the expression of RPL5 and RPL11 to directly bind to MDM2 in HCT116 cells. Conversely, deletion of RPL5 and RPL11 blocked the activation of p53, p21, and MDM2 in HCT116 cells. Also, puromycin enhanced the antitumor effect with reactivating p53 and inducing tumor apoptosis (RITA) or doxorubicin in HCT116 cells. These findings suggest that puromycin induces p53-dependent apoptosis via upregulation of RPL5 or RPL11 for binding with MDM2, and so can be used more effectively in p53 wild-type cancers by combination with RITA or doxorubicin.

scholarly journals Developmental expression and 5S rRNA-binding activity of Xenopus laevis ribosomal protein L5.

1989 ◽  
Vol 9 (12) ◽  
pp. 5281-5288 ◽  
Author(s):  
W M Wormington
Keyword(s):  
Ribosomal Protein ◽  
Mammalian Cells ◽  
Ribosomal Proteins ◽  
5S Rrna ◽  
Yeast Cells ◽  
Developmental Expression ◽  
Rrna Synthesis ◽  
Ribosome Assembly ◽  
Subunit Assembly ◽  
Ribosomal Protein L5

Ribosomal protein L5 binds specifically to 5S rRNA to form a complex that is a precursor to 60S subunit assembly in vivo. Analyses in yeast cells, mammalian cells, and Xenopus embryos have shown that the accumulation of L5 is not coordinated with the expression of other ribosomal proteins. In this study, the primary structure and developmental expression of Xenopus ribosomal protein L5 were examined to determine the basis for its distinct regulation. These analyses showed that L5 expression could either coincide with 5S rRNA synthesis and ribosome assembly or be controlled independently of these events at different stages of Xenopus development. L5 synthesis during oogenesis was uncoupled from the accumulation of 5S rRNa but coincided with subunit assembly. In early embryos, the inefficient translation of L5 mRNA resulted in the accumulation of a stable L5-5S rRNA complex before ribosome assembly at later stages of development. Additional results demonstrated that L5 protein synthesized in vitro bound specifically to 5S rRNA.

scholarly journals Ribosomal protein L5 has a highly twisted concave surface and flexible arms responsible for rRNA binding

RNA ◽  
2001 ◽  
Vol 7 (5) ◽  
pp. 692-701 ◽  
Author(s):  
TAKASHI NAKASHIMA ◽  
MIN YAO ◽  
SHUNSUKE KAWAMURA ◽  
KENTA IWASAKI ◽  
MAKOTO KIMURA ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Concave Surface ◽  
Ribosomal Protein L5 ◽  
Flexible Arms
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