scholarly journals Conserved sequence elements upstream of the gene encoding yeast ribosomal protein L25 are involved in transcription activation.

1986 ◽  
Vol 5 (5) ◽  
pp. 1037-1040 ◽  
Author(s):  
L.P. Woudt ◽  
A.B. Smit ◽  
W.H. Mager ◽  
R.J. Planta
Keyword(s):  
Ribosomal Protein ◽  
Transcription Activation ◽  
Gene Encoding ◽  
Conserved Sequence ◽  
Sequence Elements

Ribosomal protein S19 expression during erythroid differentiation

Blood ◽  
2003 ◽  
Vol 101 (1) ◽  
pp. 318-324 ◽  
Author(s):  
Lydie Da Costa ◽  
Goutham Narla ◽  
Thiébaut-Noel Willig ◽  
Luanne L. Peters ◽  
Marilyn Parra ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Regulatory Element ◽  
Erythroid Differentiation ◽  
Gene Encoding ◽  
Sequence Element ◽  
Conserved Sequence ◽  
Diamond Blackfan Anemia ◽  
Sequence Elements ◽  
Ribosomal Protein S19 ◽  
Terminal Erythroid Differentiation

Abstract The gene encoding ribosomal protein S19 (RPS19) has been shown to be mutated in 25% of the patients affected by Diamond-Blackfan anemia (DBA), a congenital erythroblastopenia. As the role of RPS19 in erythropoiesis is still to be defined, we performed studies on RPS19 expression during terminal erythroid differentiation. Comparative analysis of the genomic sequences of human and mouse RPS19genes enabled the identification of 4 conserved sequence elements in the 5′ region. Characterization of transcriptional elements allowed the identification of the promoter in the human RPS19 gene and the localization of a strong regulatory element in the third conserved sequence element. By Northern blot and Western blot analyses of murine splenic erythroblasts infected with the anemia-inducing strain Friend virus (FAV cells), RPS19 mRNA and protein expression were shown to decrease during terminal erythroid differentiation. We anticipate that these findings will contribute to further development of our understanding of the contribution of RPS19 to erythropoiesis.

scholarly journals Olfactory expression of trace amine-associated receptors requires cooperative cis-acting enhancers

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Ami Shah ◽  
Madison Ratkowski ◽  
Alessandro Rosa ◽  
Paul Feinstein ◽  
Thomas Bozza
Keyword(s):  
Gene Expression ◽  
Large Family ◽  
Sequence Motifs ◽  
Specific Expression ◽  
Cis Acting ◽  
Conserved Sequence ◽  
Trace Amine ◽  
Sequence Elements ◽  
Cell Type Specific Expression ◽  
Cell Type Specific

AbstractOlfactory sensory neurons express a large family of odorant receptors (ORs) and a small family of trace amine-associated receptors (TAARs). While both families are subject to so-called singular expression (expression of one allele of one gene), the mechanisms underlying TAAR gene choice remain obscure. Here, we report the identification of two conserved sequence elements in the mouse TAAR cluster (T-elements) that are required for TAAR gene expression. We observed that cell-type-specific expression of a TAAR-derived transgene required either T-element. Moreover, deleting either element reduced or abolished expression of a subset of TAAR genes, while deleting both elements abolished olfactory expression of all TAARs in cis with the mutation. The T-elements exhibit several features of known OR enhancers but also contain highly conserved, unique sequence motifs. Our data demonstrate that TAAR gene expression requires two cooperative cis-acting enhancers and suggest that ORs and TAARs share similar mechanisms of singular expression.

scholarly journals Identification of a gene encoding the predicted ribosomal protein L7b divergently transcribed fromPOL1in fission yeastSchizosaccharomyces pombe

1991 ◽  
Vol 19 (5) ◽  
pp. 1099-1104 ◽  
Author(s):  
Véronigue Damagnez ◽  
Anne-Marie de Recondo ◽  
Guiseppe Baldacci
Keyword(s):  
Ribosomal Protein ◽  
Gene Encoding

A short conserved sequence is involved in the light-inducibility of a gene encoding ribulose 1,5-bisphosphate carboxylase small subunit of pea

Nature ◽  
1985 ◽  
Vol 315 (6016) ◽  
pp. 200-204 ◽  
Author(s):  
Giorgio Morelli ◽  
Ferenc Nagy ◽  
Robert T. Fraley ◽  
Stephen G. Rogers ◽  
Nam-Hai Chua
Keyword(s):  
Small Subunit ◽  
Gene Encoding ◽  
Bisphosphate Carboxylase ◽  
Conserved Sequence ◽  
Light Inducibility

scholarly journals Transcription Activation Domains of the Yeast Factors Met4 and Ino2: Tandem Activation Domains with Properties Similar to the Yeast Gcn4 Activator

2018 ◽  
Vol 38 (10) ◽  
Author(s):  
Derek Pacheco ◽  
Linda Warfield ◽  
Michelle Brajcich ◽  
Hannah Robbins ◽  
Jie Luo ◽  
...  
Keyword(s):  
Transcription Initiation ◽  
Transcription Activation ◽  
Binding Studies ◽  
Eukaryotic Transcription ◽  
Activation Domains ◽  
Conserved Sequence ◽  
Functional Studies ◽  
Intrinsically Disordered ◽  
Binding Domains ◽  
Optimal Function

ABSTRACTEukaryotic transcription activation domains (ADs) are intrinsically disordered polypeptides that typically interact with coactivator complexes, leading to stimulation of transcription initiation, elongation, and chromatin modifications. Here we examined the properties of two strong and conserved yeast ADs: Met4 and Ino2. Both factors have tandem ADs that were identified by conserved sequence and functional studies. While the AD function of both factors depended on hydrophobic residues, Ino2 further required key conserved acidic and polar residues for optimal function. Binding studies showed that the ADs bound multiple Med15 activator-binding domains (ABDs) with similar orders of micromolar affinity and similar but distinct thermodynamic properties. Protein cross-linking data show that no unique complex was formed upon Met4-Med15 binding. Rather, we observed heterogeneous AD-ABD contacts with nearly every possible AD-ABD combination. Many of these properties are similar to those observed with yeast activator Gcn4, which forms a large heterogeneous, dynamic, and fuzzy complex with Med15. We suggest that this molecular behavior is common among eukaryotic activators.

Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits

1993 ◽  
Vol 13 (5) ◽  
pp. 2835-2845
Author(s):  
M Deshmukh ◽  
Y F Tsay ◽  
A G Paulovich ◽  
J L Woolford
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Subunit ◽  
Single Copy ◽  
5S Rrna ◽  
Gene Encoding ◽  
Ribosomal Subunits ◽  
Ribosomal Protein L1 ◽  
The Stability ◽  
And Function

Ribosomal protein L1 from Saccharomyces cerevisiae binds 5S rRNA and can be released from intact 60S ribosomal subunits as an L1-5S ribonucleoprotein (RNP) particle. To understand the nature of the interaction between L1 and 5S rRNA and to assess the role of L1 in ribosome assembly and function, we cloned the RPL1 gene encoding L1. We have shown that RPL1 is an essential single-copy gene. A conditional null mutant in which the only copy of RPL1 is under control of the repressible GAL1 promoter was constructed. Depletion of L1 causes instability of newly synthesized 5S rRNA in vivo. Cells depleted of L1 no longer assemble 60S ribosomal subunits, indicating that L1 is required for assembly of stable 60S ribosomal subunits but not 40S ribosomal subunits. An L1-5S RNP particle not associated with ribosomal particles was detected by coimmunoprecipitation of L1 and 5S rRNA. This pool of L1-5S RNP remained stable even upon cessation of 60S ribosomal subunit assembly by depletion of another ribosomal protein, L16. Preliminary results suggest that transcription of RPL1 is not autogenously regulated by L1.

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