scholarly journals Integrative analyses shed new light on human ribosomal protein gene regulation

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Xin Li ◽  
Yiyu Zheng ◽  
Haiyan Hu ◽  
Xiaoman Li
Keyword(s):  
Gene Regulation ◽  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Integrative Analyses ◽  
Human Ribosomal Protein

Identification of highly specific localized sequence motifs in human ribosomal protein gene promoters

Gene ◽  
2006 ◽  
Vol 365 ◽  
pp. 48-56 ◽  
Author(s):  
Stefan Roepcke ◽  
Degui Zhi ◽  
Martin Vingron ◽  
Peter F. Arndt
Keyword(s):  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Gene Promoters ◽  
Sequence Motifs ◽  
Human Ribosomal Protein

Fine-structure map of the human ribosomal protein gene RPS14

1992 ◽  
Vol 12 (4) ◽  
pp. 1680-1686
Author(s):  
J J Diaz ◽  
D J Roufa
Keyword(s):  
Biological Activity ◽  
Fine Structure ◽  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Genetic Maps ◽  
Chemical Mutagenesis ◽  
In Vitro Mutagenesis ◽  
Amino Terminal ◽  
Human Ribosomal Protein

We have used polymerase chain reaction-mediated chemical mutagenesis (J.-J. Diaz, D. D. Rhoads, and D. J. Roufa, BioTechniques 11:204-211, 1991) to analyze the genetic fine structure of a human ribosomal protein gene, RPS14. Eighty-three DNA clones containing 158 random single-base substitution mutations were isolated. Mutant RPS14 alleles were tested for biological activity by transfection into cultured Chinese hamster cells. The resulting data permitted us to construct a map of the S14-coding sequence that is comparable to available fine-structure genetic maps of many prokaryotic and lower eukaryotic gene loci. As predicted from the multiplicity of protein-protein and protein-RNA interactions required for ribosomal protein transport and assembly into functional ribosomal subunits, the distribution of null mutations indicated that S14 is composed of multiple, functionally distinct polypeptide domains. Two of the protein's internal domains, designated domains B and D, were essential for S14 biological activity. In contrast, mutations which altered or deleted S14's amino-terminal 20 amino acid residues (domain A) had no observable effect on the protein's assembly and function in mammalian ribosomes. Interestingly, S14 structural domains deduced by in vitro mutagenesis correlate well with the RPS14 gene's exon boundaries.

scholarly journals Gene duplication and the evolution of ribosomal protein gene regulation in yeast

2010 ◽  
Vol 107 (12) ◽  
pp. 5505-5510 ◽  
Author(s):  
I. Wapinski ◽  
J. Pfiffner ◽  
C. French ◽  
A. Socha ◽  
D. A. Thompson ◽  
...  
Keyword(s):  
Gene Regulation ◽  
Gene Duplication ◽  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene

scholarly journals Fine-structure map of the human ribosomal protein gene RPS14.

1992 ◽  
Vol 12 (4) ◽  
pp. 1680-1686 ◽  
Author(s):  
J J Diaz ◽  
D J Roufa
Keyword(s):  
Biological Activity ◽  
Fine Structure ◽  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Genetic Maps ◽  
Chemical Mutagenesis ◽  
In Vitro Mutagenesis ◽  
Amino Terminal ◽  
Human Ribosomal Protein

We have used polymerase chain reaction-mediated chemical mutagenesis (J.-J. Diaz, D. D. Rhoads, and D. J. Roufa, BioTechniques 11:204-211, 1991) to analyze the genetic fine structure of a human ribosomal protein gene, RPS14. Eighty-three DNA clones containing 158 random single-base substitution mutations were isolated. Mutant RPS14 alleles were tested for biological activity by transfection into cultured Chinese hamster cells. The resulting data permitted us to construct a map of the S14-coding sequence that is comparable to available fine-structure genetic maps of many prokaryotic and lower eukaryotic gene loci. As predicted from the multiplicity of protein-protein and protein-RNA interactions required for ribosomal protein transport and assembly into functional ribosomal subunits, the distribution of null mutations indicated that S14 is composed of multiple, functionally distinct polypeptide domains. Two of the protein's internal domains, designated domains B and D, were essential for S14 biological activity. In contrast, mutations which altered or deleted S14's amino-terminal 20 amino acid residues (domain A) had no observable effect on the protein's assembly and function in mammalian ribosomes. Interestingly, S14 structural domains deduced by in vitro mutagenesis correlate well with the RPS14 gene's exon boundaries.

scholarly journals Cloning and charaterization of a human ribosomal protein gene with enhanced expression in fetal and neoplastic cells

1987 ◽  
Vol 15 (21) ◽  
pp. 8919-8934 ◽  
Author(s):  
Jing-hsiung Ou ◽  
T.S.Benedict Yen ◽  
Yan-Fei Wang ◽  
Wing K. Kam ◽  
William J. Rutter
Keyword(s):  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Neoplastic Cells ◽  
Enhanced Expression ◽  
Human Ribosomal Protein

A cloned human ribosomal protein gene functions in rodent cells

1987 ◽  
Vol 7 (10) ◽  
pp. 3767-3774
Author(s):  
D D Rhoads ◽  
D J Roufa
Keyword(s):  
Ribosomal Protein ◽  
Cho Cells ◽  
Protein Gene ◽  
Chinese Hamster ◽  
Ribosomal Protein Gene ◽  
Mrna Levels ◽  
Flanking Sequence ◽  
Base Pairs ◽  
Exon 1 ◽  
Human Ribosomal Protein

Cloned fragments of human ribosomal protein S14 DNA (RPS14) were transfected into cultured Chinese hamster (CHO) cells. Transient expression assays indicated that DNA with as little as 31 base pairs of upstream flanking sequence was transcribed into a polyadenylated, 650-base mRNA that is largely bound to the polyribosomes. In these respects the exogenous human S14 message appeared to function normally in CHO cells. Interestingly, transcription of human RPS14 did not require the TATA sequence located 26 base pairs upstream of exon 1. Stably transformed clones were selected from cultures of emetine-resistant CHO cells (Emr-2) after transfection with pSV2Neo-human RPS14 constructs. Human RPS14 complemented the mutationally based drug resistance of the Chinese hamster cells, demonstrating that the cloned human ribosomal protein gene is functional in rodent cells. Analysis of transformed cells with different amounts of integrated RPS14 indicated that human S14 mRNA levels are not tightly regulated by CHO cells. In contrast, the steady-state S14 level fluctuated only slightly, if at all, in transformed clones whose S14 message contents differed by more than 30-fold. These data support the conclusion that expression of human RPS14 is regulated, at least partially, posttranscriptionally.

scholarly journals Cloning and characterization of a human ribosomal protein gene with enhanced expression in fetal and neoplastic cells

1988 ◽  
Vol 16 (9) ◽  
pp. 4196-4196 ◽  
Author(s):  
Jing-hsing Ou ◽  
T.S.Benedict Yen ◽  
Yan-Fei Wang ◽  
Wing K. Kam ◽  
William J. Rutter
Keyword(s):  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Neoplastic Cells ◽  
Enhanced Expression ◽  
Human Ribosomal Protein

Multiple regulatory elements ensure accurate transcription of a human ribosomal protein gene

1993 ◽  
Vol 19 (4) ◽  
pp. 347-362 ◽  
Author(s):  
Paul F. Overman ◽  
Douglas D. Rhoads ◽  
Elena S. Tasheva ◽  
Marla M. Pyle ◽  
Donald J. Roufa
Keyword(s):  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Regulatory Elements ◽  
Human Ribosomal Protein

scholarly journals A cloned human ribosomal protein gene functions in rodent cells.

1987 ◽  
Vol 7 (10) ◽  
pp. 3767-3774 ◽  
Author(s):  
D D Rhoads ◽  
D J Roufa
Keyword(s):  
Ribosomal Protein ◽  
Cho Cells ◽  
Protein Gene ◽  
Chinese Hamster ◽  
Ribosomal Protein Gene ◽  
Mrna Levels ◽  
Flanking Sequence ◽  
Base Pairs ◽  
Exon 1 ◽  
Human Ribosomal Protein

Cloned fragments of human ribosomal protein S14 DNA (RPS14) were transfected into cultured Chinese hamster (CHO) cells. Transient expression assays indicated that DNA with as little as 31 base pairs of upstream flanking sequence was transcribed into a polyadenylated, 650-base mRNA that is largely bound to the polyribosomes. In these respects the exogenous human S14 message appeared to function normally in CHO cells. Interestingly, transcription of human RPS14 did not require the TATA sequence located 26 base pairs upstream of exon 1. Stably transformed clones were selected from cultures of emetine-resistant CHO cells (Emr-2) after transfection with pSV2Neo-human RPS14 constructs. Human RPS14 complemented the mutationally based drug resistance of the Chinese hamster cells, demonstrating that the cloned human ribosomal protein gene is functional in rodent cells. Analysis of transformed cells with different amounts of integrated RPS14 indicated that human S14 mRNA levels are not tightly regulated by CHO cells. In contrast, the steady-state S14 level fluctuated only slightly, if at all, in transformed clones whose S14 message contents differed by more than 30-fold. These data support the conclusion that expression of human RPS14 is regulated, at least partially, posttranscriptionally.

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