scholarly journals RNA polymerase II components and Rrn7 form a preinitiation complex on the HomolD box to promote ribosomal protein gene expression inSchizosaccharomyces pombe

FEBS Journal ◽  
2017 ◽  
Vol 284 (4) ◽  
pp. 615-633 ◽  
Author(s):  
Matías Montes ◽  
Sandra Moreira-Ramos ◽  
Diego A. Rojas ◽  
Fabiola Urbina ◽  
Norbert F. Käufer ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rna Polymerase ◽  
Ribosomal Protein ◽  
Rna Polymerase Ii ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Preinitiation Complex

Association of RAP1 binding sites with stringent control of ribosomal protein gene transcription in Saccharomyces cerevisiae

1991 ◽  
Vol 11 (5) ◽  
pp. 2723-2735 ◽  
Author(s):  
C M Moehle ◽  
A G Hinnebusch
Keyword(s):  
Gene Expression ◽  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Ribosomal Protein ◽  
Binding Sites ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Ribosomal Protein Genes ◽  
Biosynthetic Genes ◽  
Stringent Control

An amino acid limitation in bacteria elicits a global response, called stringent control, that leads to reduced synthesis of rRNA and ribosomal proteins and increased expression of amino acid biosynthetic operons. We have used the antimetabolite 3-amino-1,2,4-triazole to cause histidine limitation as a means to elicit the stringent response in the yeast Saccharomyces cerevisiae. Fusions of the yeast ribosomal protein genes RPL16A, CRY1, RPS16A, and RPL25 with the Escherichia coli lacZ gene were used to show that the expression of these genes is reduced by a factor of 2 to 5 during histidine-limited exponential growth and that this regulation occurs at the level of transcription. Stringent regulation of the four yeast ribosomal protein genes was shown to be associated with a nucleotide sequence, known as the UASrpg (upstream activating sequence for ribosomal protein genes), that binds the transcriptional regulatory protein RAP1. The RAP1 binding sites also appeared to mediate the greater ribosomal protein gene expression observed in cells growing exponentially than in cells in stationary phase. Although expression of the ribosomal protein genes was reduced in response to histidine limitation, the level of RAP1 DNA-binding activity in cell extracts was unaffected. Yeast strains bearing a mutation in any one of the genes GCN1 to GCN4 are defective in derepression of amino acid biosynthetic genes in 10 different pathways under conditions of histidine limitation. These Gcn- mutants showed wild-type regulation of ribosomal protein gene expression, which suggests that separate regulatory pathways exist in S. cerevisiae for the derepression of amino acid biosynthetic genes and the repression of ribosomal protein genes in response to amino acid starvation.

scholarly journals Defective Ribosomal Protein Gene Expression Alters Transcription, Translation, Apoptosis, and Oncogenic Pathways in Diamond-Blackfan Anemia

Stem Cells ◽  
2006 ◽  
Vol 24 (9) ◽  
pp. 2034-2044 ◽  
Author(s):  
Hanna T. Gazda ◽  
Alvin T. Kho ◽  
Despina Sanoudou ◽  
Jan M. Zaucha ◽  
Isaac S. Kohane ◽  
...  
Keyword(s):  
Gene Expression ◽  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Diamond Blackfan Anemia ◽  
Oncogenic Pathways

scholarly journals MYSM1 maintains ribosomal protein gene expression in hematopoietic stem cells to prevent hematopoietic dysfunction

JCI Insight ◽  
2020 ◽  
Vol 5 (13) ◽  
Author(s):  
Jad I. Belle ◽  
HanChen Wang ◽  
Amanda Fiore ◽  
Jessica C. Petrov ◽  
Yun Hsiao Lin ◽  
...  
Keyword(s):  
Gene Expression ◽  
Stem Cells ◽  
Hematopoietic Stem Cells ◽  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene ◽  
Hematopoietic Stem

Coordinated Changes in Classes of Ribosomal Protein Gene Expression Is Associated with Light-Induced Retinal Degeneration

2004 ◽  
Vol 45 (11) ◽  
pp. 3885 ◽  
Author(s):  
Ruby Grewal ◽  
Jadwiga Stepczynski ◽  
Rhonda Kelln ◽  
Timothy Erickson ◽  
Ruth Darrow ◽  
...  
Keyword(s):  
Gene Expression ◽  
Ribosomal Protein ◽  
Retinal Degeneration ◽  
Protein Gene ◽  
Ribosomal Protein Gene

Characterization of a mammalian ribosomal protein gene promoter

1990 ◽  
Vol 68 (6) ◽  
pp. 949-956 ◽  
Author(s):  
Peter Zahradka ◽  
Dawn E. Larson ◽  
Bruce H. Sells
Keyword(s):  
Ribosomal Protein ◽  
Rna Polymerase Ii ◽  
Dihydrofolate Reductase ◽  
Protein Gene ◽  
Gene Promoter ◽  
Ribosomal Protein Gene ◽  
Late Promoter ◽  
Promoter Elements ◽  
Adenovirus Major Late Promoter ◽  
Major Late Promoter

The presence of specific promoter elements, notably the TATA and GC boxes, has been useful for categorizing genes transcribed by RNA polymerase II. The gene for the murine ribosomal protein (r-protein) L32 lacks both of these elements, although it has GC-rich regions. The conditions required for its optimal synthesis in vitro, however, resemble the properties of promoters containing TATA (adenovirus major late promoter) rather than GC boxes (dihydrofolate reductase). To further investigate the relationship of the r-protein gene to different promoter elements, transcription competition analyses were used to distinguish the presence of common protein-binding sequences. The low levels of competition observed by either the adenovirus major late promoter or dihydrofolate reductase promoter with the r-protein gene promoter resulted from general transcription factors present in each initiation complex. Competition by factors binding to common sequence elements was not observed, indicating the r-protein L32 gene possesses elements distinct from those present in the other genes examined.Key words: ribosomal protein gene, gene promoter, cell-free transcription.

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