The Primary Structure of Rat Ribosomal Protein S15a

Chan, Yuen‐Ling; Olvera, Joe; Paz, Veronica; Wool, Ira G.

doi:10.1006/bbrc.1994.1620

Cited by 16 publications

(12 citation statements)

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“…S22051) and rat S15a [35] at positions 33-37 where differences were found: human S15a (this study), rat S15a (PIR accession no. JC2234), human S15a (PIR accession no.…”

Section: Discussionsupporting

confidence: 48%

Characterization of the Human Small‐Ribosomal‐Subunit Proteins by N‐Terminal and Internal Sequencing, and Mass Spectrometry

Vladimirov

Ivanov

Карпова

et al. 1996

European Journal of Biochemistry

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Reverse-phase HPLC was used to fractionate 40s ribosomal proteins from human placenta. Application of a C, reverse-phase column allowed us to obtain 27 well-resolved peaks. The protein composition of each chromatographic fraction was established by two-dimensional polyacrylamide gel electrophoresis and N-terminal sequencing. N-terminally blocked proteins were cleaved with endoproteinase Lys-C, and suitable peptides were sequenced. All sequences were compared with those of ribosomal proteins available from data bases. This allowed us to identify all proteins from the 40s human ribosomal subunit in the HPLC elution profile. By matrix-assisted laser-desorption ionization mass spectrometry the masses of the 40s proteins were determined and checked for the presence of post-translational modifications. For several proteins differences to the deduced sequences and the calculated masses were found to be due to post-translational modifications.Keywords: human ribosomal proteins ; HPLC ; N-terminal and internal amino acid sequencing ; matrixassisted-laser-desorption ionization MS ; post-translational modifications.Human ribosornd proteins are the main components of the fundamental processes which translate genetic information into proteins at the ribosome. Some ribosomal proteins (rp) are further involved in non-ribosomal functions. Recently, rp L7 was shown to contain the basic-region-leucine-zipper sequence which mediates the stable binding of this protein to DNA [I]. Moreover, rp S3 was found to act as an endonuclease in the DNA-repairing system [2]. Finally, some data indicate that tumor diseases may be accompanied by overexpression of rp genes 13, 4) and by chromosomal rearrangements in regions of rp genes [ S ] . Therefore, structural analysis of these proteins is necessary for complete understanding of their fundamental role in the cell. The task of structure determination of rat rp has been almost fully resolved by the application of recombinant-DNA technology ; details are reviewed in [6]. However, knowledge of the cDNA sequences does not provide information concerning post-translational modifications of the proteins after their biosynthesis and assembly into the ribosomal subunits. Several modifications of rp have been determined in the eubacterial ribosome [7, 81, and the eukaryotic rprotein S6 is known to be phosphorylated 191. This phosphorylation was shown to be connected with cell growth [I 01 and cell cycle control [I I]. At least seven 40s proteins from HeLa cells were found to be methylated, and the level of their methylation was shown to be altered in the Abbreviations. MALDI, matrix-assisted laser-desorption ionization ; Lys-C, endoproteinase Lys-C; RP, reverse-phase; rp, ribosomal protein ; S-proteins, proteins of the small ribosomal subunit; 40S, small ribosomal subunit; TP40, total protein mixture of the small ribosomal subunit; TOF, time-of-flight ; Pth-Xaa, phenylthiohydantoin -amino-acid.course of the cell cycle [12]. It is also known that ribosomal proteins may be acetylated 17, 13, 141. However...

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“…S22051) and rat S15a [35] at positions 33-37 where differences were found: human S15a (this study), rat S15a (PIR accession no. JC2234), human S15a (PIR accession no.…”

Section: Discussionsupporting

confidence: 48%

Characterization of the Human Small‐Ribosomal‐Subunit Proteins by N‐Terminal and Internal Sequencing, and Mass Spectrometry

Vladimirov

Ivanov

Карпова

et al. 1996

European Journal of Biochemistry

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“…[5][6][7] RPS15A has been shown to be upregulated in response to the Myc oncogenic transcription factor or transforming growth factor-b induction. 8,9 Recent studies have indicated that RPS15A is implicated in several human cancers.…”

Section: Introductionmentioning

confidence: 99%

Retracted: Ribosomal Protein S15A Augments Human Osteosarcoma Cell Proliferation In Vitro

Zhang

Song

et al. 2014

Cancer Biotherapy and Radiopharmaceuticals

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As a highly conserved housekeeping gene, the biological implications of ribosomal protein S15A (RPS15A) during various processes, including carcinogenesis, remain elusive. Herein, the authors reported that knockdown of RPS15A expression significantly inhibited human osteosarcoma U2OS cell proliferation and colony formation in vitro by using a lentivirus-mediated RNA interference (RNAi) system. Moreover, an excess accumulation of cells in the G0/G1 phase was observed in U2OS cells transduced with lentivirus targeting RPS15A, suggesting that the growth inhibition mediated by RPS15A knockdown in osteosarcoma cells was probably due to the induction of cell cycle arrest. Taken together, this study highlights the crucial role of RPS15A in promoting osteosarcoma cell proliferation, and provides a foundation for further study into the clinical potential of inhibition of RPS15A for the treatment of osteosarcoma.

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“…These data have revealed the putative pathways whereby HBxAg mediates transformation but do not identify the natural effectors of HBxAg that mediate these changes at the molecular and cellular levels. In this study, HBxAg was shown to upregulate expression of the ribosomal protein S15a, a highly conserved protein [19–21] that promotes mRNA/ribosome interactions early in translation [22]. S15a stimulates growth in yeast [23,24], in plants [25,26], and in human lung carcinoma cells [27], suggesting it may do the same in the context of carcinogenesis.…”

Section: Introductionmentioning

confidence: 99%

Human S15a expression is upregulated by hepatitis B virus X protein

Lian

Liu

et al. 2004

Molecular Carcinogenesis

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The hepatitis B virus (HBV)-encoded X antigen (HBxAg) may contribute to the development of hepatocellular carcinoma (HCC) through the upregulated expression of selected cellular genes. To identify these genes, RNAs isolated from HBxAg-positive and -negative HepG2 cells were compared by PCR select cDNA subtraction. One gene overexpressed in HBxAg-positive cells by Northern and Western blotting is the ribosomal protein S15a. The S15a mRNA is 535 base pairs, encoding a protein 130 amino acids long with a molecular weight of 14.3 kDa. S15a expression was upregulated in HBV-infected livers, where it costained with HBxAg. Overexpression of S15a stimulated cell growth, colony formation in soft agar, and tumor formation in SCID mice. Hence, HBxAg upregulated the expression of S15a, the latter of which participates in the development of HCC, perhaps by altering the integrity of translation.

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The Primary Structure of Rat Ribosomal Protein S15a

Cited by 16 publications

References 0 publications

Characterization of the Human Small‐Ribosomal‐Subunit Proteins by N‐Terminal and Internal Sequencing, and Mass Spectrometry

Characterization of the Human Small‐Ribosomal‐Subunit Proteins by N‐Terminal and Internal Sequencing, and Mass Spectrometry

Retracted: Ribosomal Protein S15A Augments Human Osteosarcoma Cell Proliferation In Vitro

Human S15a expression is upregulated by hepatitis B virus X protein

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