scholarly journals Role of Human Ribosomal RNA (rRNA) Promoter Methylation and of Methyl-CpG-binding Protein MBD2 in the Suppression of rRNA Gene Expression

2003 ◽  
Vol 279 (8) ◽  
pp. 6783-6793 ◽  
Author(s):  
Kalpana Ghoshal ◽  
Sarmila Majumder ◽  
Jharna Datta ◽  
Tasneem Motiwala ◽  
Shoumei Bai ◽  
...  
Keyword(s):  
Gene Expression ◽  
Ribosomal Rna ◽  
Promoter Methylation ◽  
Binding Protein ◽  
Rrna Gene

scholarly journals KH-type splicing regulatory protein is a new component of chromatoid body

Reproduction ◽  
2017 ◽  
Vol 154 (6) ◽  
pp. 723-733 ◽  
Author(s):  
Huijuan Zhang ◽  
Guishuan Wang ◽  
Lin Liu ◽  
Xiaolin Liang ◽  
Yu Lin ◽  
...  
Keyword(s):  
Gene Expression ◽  
Germ Cell ◽  
Knockout Mice ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Somatic Cells ◽  
Chromatoid Body ◽  
Mechanistic Insight ◽  
Insight Into

The chromatoid body (CB) is a specific cloud-like structure in the cytoplasm of haploid spermatids. Recent findings indicate that CB is identified as a male germ cell-specific RNA storage and processing center, but its function has remained elusive for decades. In somatic cells, KH-type splicing regulatory protein (KSRP) is involved in regulating gene expression and maturation of select microRNAs (miRNAs). However, the function of KSRP in spermatogenesis remains unclear. In this study, we showed that KSRP partly localizes in CB, as a component of CB. KSRP interacts with proteins (mouse VASA homolog (MVH), polyadenylate-binding protein 1 (PABP1) and polyadenylate-binding protein 2 (PABP2)), mRNAs (Tnp2 and Odf1) and microRNAs (microRNA-182) in mouse CB. Moreover, KSRP may regulate the integrity of CB via DDX5-miRNA-182 pathway. In addition, we found abnormal expressions of CB component in testes of Ksrp-knockout mice and of patients with hypospermatogenesis. Thus, our results provide mechanistic insight into the role of KSRP in spermatogenesis.

The role of a conserved dodecamer sequence in yeast mitochondrial gene expression

Genome ◽  
1989 ◽  
Vol 31 (2) ◽  
pp. 757-760 ◽  
Author(s):  
Ronald A. Butow ◽  
Hong Zhu ◽  
Philip Perlman ◽  
Heather Conrad-Webb
Keyword(s):  
Gene Expression ◽  
Rna Processing ◽  
Mitochondrial Gene ◽  
Rna Stability ◽  
Rrna Gene ◽  
Mitochondrial Gene Expression ◽  
Reading Frame ◽  
Multicomponent Complex ◽  
Var1 Gene

All mRNAs on the yeast mitochondrial genome terminate at a conserved dodecamer sequence 5′-AAUAAUAUUCUU-3′. We have characterized two mutants with altered dodecamers. One contains a deletion of the dodecamer at the end of the var1 gene, and the other contains two adjacent transversions in the dodecamer at the end of the reading frame of fit1, a gene within the ω+ allele of the 21S rRNA gene. In each mutant, expression of the respective gene is blocked completely. A dominant nuclear suppressor, SUV3-1, was isolated that suppresses the var1 deletion but is without effect on the fit1 dodecamer mutations. Unexpectedly, however, we found that SUV3-1 blocks expression of the wild-type fit1 allele by blocking processing at its dodecamer. SUV3-1 has pleiotropic effects on mitochondrial gene expression, affecting RNA processing, RNA stability, and translation. Our results suggest that RNA metabolism and translation may be part of a multicomponent complex within mitochondria.Key words: mitochondria, yeast, mRNA, RNA processing, 3′ dodecamer.

Poly(A)-binding protein (PABP): a common viral target

2010 ◽  
Vol 426 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Richard W. P. Smith ◽  
Nicola K. Gray
Keyword(s):  
Gene Expression ◽  
Binding Protein ◽  
Intracellular Localization ◽  
Mrna Translation ◽  
Dna Viruses ◽  
Multifunctional Protein ◽  
Wide Range ◽  
Viral Target ◽  
Rna And Dna

Cytoplasmic PABP [poly(A)-binding protein] is a multifunctional protein with well-studied roles in mRNA translation and stability. In the present review, we examine recent evidence that the activity of PABP is altered during infection with a wide range of viruses, bringing about changes in its stability, complex formation and intracellular localization. Targeting of PABP by both RNA and DNA viruses highlights the role of PABP as a central regulator of gene expression.

scholarly journals 5-hydroxymethylcytosine accumulation in postmitotic neurons results in functional demethylation of expressed genes

2017 ◽  
Vol 114 (37) ◽  
pp. E7812-E7821 ◽  
Author(s):  
Marian Mellén ◽  
Pinar Ayata ◽  
Nathaniel Heintz
Keyword(s):  
Gene Expression ◽  
Binding Protein ◽  
Binding Specificity ◽  
Chromatin Organization ◽  
Postmitotic Neurons ◽  
Cg Dinucleotides

5-hydroxymethylcytosine (5hmC) occurs at maximal levels in postmitotic neurons, where its accumulation is cell-specific and correlated with gene expression. Here we demonstrate that the distribution of 5hmC in CG and non-CG dinucleotides is distinct and that it reflects the binding specificity and genome occupancy of methylcytosine binding protein 2 (MeCP2). In expressed gene bodies, accumulation of 5hmCG acts in opposition to 5mCG, resulting in “functional” demethylation and diminished MeCP2 binding, thus facilitating transcription. Non-CG hydroxymethylation occurs predominantly in CA dinucleotides (5hmCA) and it accumulates in regions flanking active enhancers. In these domains, oxidation of 5mCA to 5hmCA does not alter MeCP2 binding or expression of adjacent genes. We conclude that the role of 5-hydroxymethylcytosine in postmitotic neurons is to functionally demethylate expressed gene bodies while retaining the role of MeCP2 in chromatin organization.

Evidence for the role of promoter methylation in the regulation of MMP-9 gene expression

2002 ◽  
Vol 297 (4) ◽  
pp. 765-772 ◽  
Author(s):  
Éric Chicoine ◽  
Pierre-Olivier Estève ◽  
Olivier Robledo ◽  
Céline Van Themsche ◽  
Edouard F Potworowski ◽  
...  
Keyword(s):  
Gene Expression ◽  
Promoter Methylation

scholarly journals Induction of utrophin gene expression by heregulin in skeletal muscle cells: Role of the N-box motif and GA binding protein

1999 ◽  
Vol 96 (6) ◽  
pp. 3223-3227 ◽  
Author(s):  
A. O. Gramolini ◽  
L. M. Angus ◽  
L. Schaeffer ◽  
E. A. Burton ◽  
J. M. Tinsley ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Binding Protein ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Ga Binding Protein

scholarly journals An RNA-binding switch drives ribosome biogenesis and tumorigenesis downstream of RAS oncogene

2021 ◽  
Author(s):  
Muhammad S Azman ◽  
Martin Dodel ◽  
Federica Capraro ◽  
Rupert Faraway ◽  
Maria Dermit ◽  
...  
Keyword(s):  
Gene Expression ◽  
Ribosomal Rna ◽  
Ribosome Biogenesis ◽  
Rna Binding ◽  
Binding Activity ◽  
Ras Signaling ◽  
Cancer Cell Proliferation ◽  
Inhibit Tumor Growth ◽  
Oncogenic Ras

Oncogenic RAS signaling reprograms gene expression through both transcriptional and post-transcriptional mechanisms. While transcriptional regulation downstream of RAS is relatively well-characterized, how RAS post-transcriptionally modulates gene expression to promote malignancy is unclear. Using quantitative RNA Interactome Capture analysis, we reveal that oncogenic RAS signaling reshapes the RNA-bound proteomic landscape of cancer cells, with a network of nuclear proteins centered around Nucleolin displaying enhanced RNA-binding activity. We show that Nucleolin is phosphorylated downstream of RAS, which increases its binding to pre-ribosomal-RNA (rRNA), boosts rRNA production, and promotes ribosome biogenesis. This Nucleolin-dependent enhancement of ribosome biogenesis is crucial for RAS-induced cancer cell proliferation, and can be targeted therapeutically to inhibit tumor growth. Our results reveal that oncogenic RAS signaling drives ribosome biogenesis by regulating the RNA-binding activity of Nucleolin, and highlights the crucial role of this process in RAS-mediated tumorigenesis.

Regulation of the intestinal mucin MUC2 gene expression in vivo: evidence for the role of promoter methylation

2001 ◽  
Vol 168 (1) ◽  
pp. 71-80 ◽  
Author(s):  
Alexei Gratchev ◽  
Anja Siedow ◽  
Christiane Bumke-Vogt ◽  
Michael Hummel ◽  
Hans-Dieter Foss ◽  
...  
Keyword(s):  
Gene Expression ◽  
Promoter Methylation ◽  
Intestinal Mucin
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