| Datasheet H3K4me3 sp003 DATASHEET Datasheet description | Download |
| Datasheet H3K4me3 C15410003 DATASHEET Datasheet description | Download |
Synthetic peptide derived from the N-terminal domain of human histone H3 containing the trimethylated lysine 4.
This peptide was used as immunogen to raise the ChIP-grade Diagenode antibody directed against H3K4me3 (Cat. No. pAb-003-050). The same peptide can be used to block this antibody in negative control experiments.
For more information about H3K4me3: see overview in the Technical Data Sheet of the ChIP-grade Diagenode antibody directed against H3K4me3 (Cat. No. pAb-003-050).
| Datasheet H3K4me3 sp003 DATASHEET Datasheet description | Download |
| Datasheet H3K4me3 C15410003 DATASHEET Datasheet description | Download |
 How to properly cite this product in your workDiagenode strongly recommends using this: H3K4me3 peptide (Diagenode Cat# C16000003). Click here to copy to clipboard. Using our products in your publication? Let us know! |
Single amino-acid mutation in a Drosoph ila melanogaster ribosomalprotein: An insight in uL11 transcriptional activity. |
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No. pAb-003-050). The same peptide can be used to block this antibody in negative control experiments. </span><br /><br /><span>For more information about H3K4me3: see overview in the Technical Data Sheet of the ChIP-grade Diagenode antibody directed against H3K4me3 (Cat. 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In addition, no mutant for uL11 is available suggesting that this gene is haplo-insufficient as many other Ribosomal Protein Genes (RPGs). We have previously shown that overexpression of Drosophila melanogaster uL11 enhances the transcription of many RPGs and Ribosomal Biogenesis genes (RiBis) suggesting that uL11 might globally regulate the level of translation through its transcriptional activity. Moreover, uL11 trimethylated on lysine 3 (uL11K3me3) interacts with the chromodomain of the Enhancer of Polycomb and Trithorax Corto, and both proteins co-localize with RNA Polymerase II at many sites on polytene chromosomes. These data have led to the hypothesis that the N-terminal end of uL11, and more particularly the trimethylation of lysine 3, supports the extra-ribosomal activity of uL11 in transcription. To address this question, we mutated the lysine 3 codon using a CRISPR/Cas9 strategy and obtained several lysine 3 mutants. 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In addition, no mutant for uL11 is available suggesting that this gene is haplo-insufficient as many other Ribosomal Protein Genes (RPGs). We have previously shown that overexpression of Drosophila melanogaster uL11 enhances the transcription of many RPGs and Ribosomal Biogenesis genes (RiBis) suggesting that uL11 might globally regulate the level of translation through its transcriptional activity. Moreover, uL11 trimethylated on lysine 3 (uL11K3me3) interacts with the chromodomain of the Enhancer of Polycomb and Trithorax Corto, and both proteins co-localize with RNA Polymerase II at many sites on polytene chromosomes. These data have led to the hypothesis that the N-terminal end of uL11, and more particularly the trimethylation of lysine 3, supports the extra-ribosomal activity of uL11 in transcription. To address this question, we mutated the lysine 3 codon using a CRISPR/Cas9 strategy and obtained several lysine 3 mutants. We describe here the first mutants of D. melanogaster uL11. Unexpectedly, the uL11K3A mutant, in which the lysine 3 codon is replaced by an alanine, displays a genuine Minute phenotype known to be characteristic of RPG deletions (longer development, low fertility, high lethality, thin and short bristles) whereas the uL11K3Y mutant, in which the lysine 3 codon is replaced by a tyrosine, is unaffected. In agreement, the rate of translation decreases in uL11K3A but not in uL11K3Y. Co-immunoprecipitation experiments show that the interaction between uL11 and the Corto chromodomain is impaired by both mutations. However, Histone Association Assays indicate that the mutant proteins still bind chromatin. RNA-seq analyses from wing imaginal discs show that Corto represses RPG expression whereas very few genes are deregulated in uL11 mutants. 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In addition, no mutant for uL11 is available suggesting that this gene is haplo-insufficient as many other Ribosomal Protein Genes (RPGs). We have previously shown that overexpression of Drosophila melanogaster uL11 enhances the transcription of many RPGs and Ribosomal Biogenesis genes (RiBis) suggesting that uL11 might globally regulate the level of translation through its transcriptional activity. Moreover, uL11 trimethylated on lysine 3 (uL11K3me3) interacts with the chromodomain of the Enhancer of Polycomb and Trithorax Corto, and both proteins co-localize with RNA Polymerase II at many sites on polytene chromosomes. These data have led to the hypothesis that the N-terminal end of uL11, and more particularly the trimethylation of lysine 3, supports the extra-ribosomal activity of uL11 in transcription. To address this question, we mutated the lysine 3 codon using a CRISPR/Cas9 strategy and obtained several lysine 3 mutants. We describe here the first mutants of D. melanogaster uL11. Unexpectedly, the uL11K3A mutant, in which the lysine 3 codon is replaced by an alanine, displays a genuine Minute phenotype known to be characteristic of RPG deletions (longer development, low fertility, high lethality, thin and short bristles) whereas the uL11K3Y mutant, in which the lysine 3 codon is replaced by a tyrosine, is unaffected. In agreement, the rate of translation decreases in uL11K3A but not in uL11K3Y. Co-immunoprecipitation experiments show that the interaction between uL11 and the Corto chromodomain is impaired by both mutations. However, Histone Association Assays indicate that the mutant proteins still bind chromatin. RNA-seq analyses from wing imaginal discs show that Corto represses RPG expression whereas very few genes are deregulated in uL11 mutants. We propose that Corto, by repressing RPG expression, ensures that all ribosomal proteins are present at the correct stoichiometry, and that uL11 fine-tunes its transcriptional regulation of RPGs.</p>', 'date' => '2022-01-01', 'pmid' => 'https://pubmed.ncbi.nlm.nih.gov/35981051/', 'doi' => '10.1371/journal.pone.0273198', 'modified' => '2022-11-21 10:40:47', 'created' => '2022-11-15 09:26:20', 'ProductsPublication' => array( [maximum depth reached] ) ) ), 'Testimonial' => array(), 'Area' => array(), 'SafetySheet' => array() ) $country = 'US' $countries_allowed = array( (int) 0 => 'CA', (int) 1 => 'US', (int) 2 => 'IE', (int) 3 => 'GB', (int) 4 => 'DK', (int) 5 => 'NO', (int) 6 => 'SE', (int) 7 => 'FI', (int) 8 => 'NL', (int) 9 => 'BE', (int) 10 => 'LU', (int) 11 => 'FR', (int) 12 => 'DE', (int) 13 => 'CH', (int) 14 => 'AT', (int) 15 => 'ES', (int) 16 => 'IT', (int) 17 => 'PT' ) $outsource = false $other_formats = array() $edit = '' $testimonials = '' $featured_testimonials = '' $related_products = '' $rrbs_service = array( (int) 0 => (int) 1894, (int) 1 => (int) 1895 ) $chipseq_service = array( (int) 0 => (int) 2683, (int) 1 => (int) 1835, (int) 2 => (int) 1836, (int) 3 => (int) 2684, (int) 4 => (int) 1838, (int) 5 => (int) 1839, (int) 6 => (int) 1856 ) $labelize = object(Closure) { } $old_catalog_number = '<br/><small><span style="color:#CCC">(sp-003-050)</span></small>' $country_code = 'US' $img = 'banners/banner-cut_tag-chipmentation-500.jpg' $label = '<img src="/img/banners/banner-customizer-back.png" alt=""/>' $document = array( 'id' => '725', 'name' => 'Datasheet H3K4me3 C15410003', 'description' => '<p>Datasheet description</p>', 'image_id' => null, 'type' => 'Datasheet', 'url' => 'files/products/antibodies/Datasheet_H3K4me3_C15410003.pdf', 'slug' => 'datasheet-h3k4me3-C15410003', 'meta_keywords' => '', 'meta_description' => '', 'modified' => '2015-11-20 17:39:34', 'created' => '2015-07-07 11:47:44', 'ProductsDocument' => array( 'id' => '409', 'product_id' => '2435', 'document_id' => '725' ) ) $publication = array( 'id' => '4510', 'name' => 'Single amino-acid mutation in a Drosoph ila melanogaster ribosomalprotein: An insight in uL11 transcriptional activity.', 'authors' => 'Grunchec H. et al.', 'description' => '<p>The ribosomal protein uL11 is located at the basis of the ribosome P-stalk and plays a paramount role in translational efficiency. In addition, no mutant for uL11 is available suggesting that this gene is haplo-insufficient as many other Ribosomal Protein Genes (RPGs). We have previously shown that overexpression of Drosophila melanogaster uL11 enhances the transcription of many RPGs and Ribosomal Biogenesis genes (RiBis) suggesting that uL11 might globally regulate the level of translation through its transcriptional activity. Moreover, uL11 trimethylated on lysine 3 (uL11K3me3) interacts with the chromodomain of the Enhancer of Polycomb and Trithorax Corto, and both proteins co-localize with RNA Polymerase II at many sites on polytene chromosomes. These data have led to the hypothesis that the N-terminal end of uL11, and more particularly the trimethylation of lysine 3, supports the extra-ribosomal activity of uL11 in transcription. To address this question, we mutated the lysine 3 codon using a CRISPR/Cas9 strategy and obtained several lysine 3 mutants. We describe here the first mutants of D. melanogaster uL11. Unexpectedly, the uL11K3A mutant, in which the lysine 3 codon is replaced by an alanine, displays a genuine Minute phenotype known to be characteristic of RPG deletions (longer development, low fertility, high lethality, thin and short bristles) whereas the uL11K3Y mutant, in which the lysine 3 codon is replaced by a tyrosine, is unaffected. In agreement, the rate of translation decreases in uL11K3A but not in uL11K3Y. Co-immunoprecipitation experiments show that the interaction between uL11 and the Corto chromodomain is impaired by both mutations. However, Histone Association Assays indicate that the mutant proteins still bind chromatin. RNA-seq analyses from wing imaginal discs show that Corto represses RPG expression whereas very few genes are deregulated in uL11 mutants. We propose that Corto, by repressing RPG expression, ensures that all ribosomal proteins are present at the correct stoichiometry, and that uL11 fine-tunes its transcriptional regulation of RPGs.</p>', 'date' => '2022-01-01', 'pmid' => 'https://pubmed.ncbi.nlm.nih.gov/35981051/', 'doi' => '10.1371/journal.pone.0273198', 'modified' => '2022-11-21 10:40:47', 'created' => '2022-11-15 09:26:20', 'ProductsPublication' => array( 'id' => '6334', 'product_id' => '2435', 'publication_id' => '4510' ) ) $externalLink = ' <a href="https://pubmed.ncbi.nlm.nih.gov/35981051/" target="_blank"><i class="fa fa-external-link"></i></a>'include - APP/View/Products/view.ctp, line 755 View::_evaluate() - CORE/Cake/View/View.php, line 971 View::_render() - CORE/Cake/View/View.php, line 933 View::render() - CORE/Cake/View/View.php, line 473 Controller::render() - CORE/Cake/Controller/Controller.php, line 963 ProductsController::slug() - APP/Controller/ProductsController.php, line 1052 ReflectionMethod::invokeArgs() - [internal], line ?? Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491 Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193 Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167 [main] - APP/webroot/index.php, line 118
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In addition, no mutant for uL11 is available suggesting that this gene is haplo-insufficient as many other Ribosomal Protein Genes (RPGs). We have previously shown that overexpression of Drosophila melanogaster uL11 enhances the transcription of many RPGs and Ribosomal Biogenesis genes (RiBis) suggesting that uL11 might globally regulate the level of translation through its transcriptional activity. Moreover, uL11 trimethylated on lysine 3 (uL11K3me3) interacts with the chromodomain of the Enhancer of Polycomb and Trithorax Corto, and both proteins co-localize with RNA Polymerase II at many sites on polytene chromosomes. These data have led to the hypothesis that the N-terminal end of uL11, and more particularly the trimethylation of lysine 3, supports the extra-ribosomal activity of uL11 in transcription. To address this question, we mutated the lysine 3 codon using a CRISPR/Cas9 strategy and obtained several lysine 3 mutants. 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In addition, no mutant for uL11 is available suggesting that this gene is haplo-insufficient as many other Ribosomal Protein Genes (RPGs). We have previously shown that overexpression of Drosophila melanogaster uL11 enhances the transcription of many RPGs and Ribosomal Biogenesis genes (RiBis) suggesting that uL11 might globally regulate the level of translation through its transcriptional activity. Moreover, uL11 trimethylated on lysine 3 (uL11K3me3) interacts with the chromodomain of the Enhancer of Polycomb and Trithorax Corto, and both proteins co-localize with RNA Polymerase II at many sites on polytene chromosomes. These data have led to the hypothesis that the N-terminal end of uL11, and more particularly the trimethylation of lysine 3, supports the extra-ribosomal activity of uL11 in transcription. To address this question, we mutated the lysine 3 codon using a CRISPR/Cas9 strategy and obtained several lysine 3 mutants. We describe here the first mutants of D. melanogaster uL11. Unexpectedly, the uL11K3A mutant, in which the lysine 3 codon is replaced by an alanine, displays a genuine Minute phenotype known to be characteristic of RPG deletions (longer development, low fertility, high lethality, thin and short bristles) whereas the uL11K3Y mutant, in which the lysine 3 codon is replaced by a tyrosine, is unaffected. In agreement, the rate of translation decreases in uL11K3A but not in uL11K3Y. Co-immunoprecipitation experiments show that the interaction between uL11 and the Corto chromodomain is impaired by both mutations. However, Histone Association Assays indicate that the mutant proteins still bind chromatin. RNA-seq analyses from wing imaginal discs show that Corto represses RPG expression whereas very few genes are deregulated in uL11 mutants. We propose that Corto, by repressing RPG expression, ensures that all ribosomal proteins are present at the correct stoichiometry, and that uL11 fine-tunes its transcriptional regulation of RPGs.</p>', 'date' => '2022-01-01', 'pmid' => 'https://pubmed.ncbi.nlm.nih.gov/35981051/', 'doi' => '10.1371/journal.pone.0273198', 'modified' => '2022-11-21 10:40:47', 'created' => '2022-11-15 09:26:20', 'ProductsPublication' => array( 'id' => '6334', 'product_id' => '2435', 'publication_id' => '4510' ) ) $externalLink = ' <a href="https://pubmed.ncbi.nlm.nih.gov/35981051/" target="_blank"><i class="fa fa-external-link"></i></a>'include - APP/View/Products/view.ctp, line 755 View::_evaluate() - CORE/Cake/View/View.php, line 971 View::_render() - CORE/Cake/View/View.php, line 933 View::render() - CORE/Cake/View/View.php, line 473 Controller::render() - CORE/Cake/Controller/Controller.php, line 963 ProductsController::slug() - APP/Controller/ProductsController.php, line 1052 ReflectionMethod::invokeArgs() - [internal], line ?? 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No. pAb-003-050).</span></p>', 'label1' => '', 'info1' => '', 'label2' => '', 'info2' => '', 'label3' => '', 'info3' => '', 'format' => '50 µg/50 µl', 'catalog_number' => 'C16000003', 'old_catalog_number' => 'sp-003-050', 'sf_code' => 'C16000003-D001-000581', 'type' => 'FRE', 'search_order' => '04-undefined', 'price_EUR' => '90', 'price_USD' => '115', 'price_GBP' => '80', 'price_JPY' => '14100', 'price_CNY' => '', 'price_AUD' => '288', 'country' => 'ALL', 'except_countries' => 'None', 'quote' => false, 'in_stock' => false, 'featured' => false, 'no_promo' => false, 'online' => true, 'master' => true, 'last_datasheet_update' => '0000-00-00', 'slug' => 'h3k4me3-peptide-50-ug-50-ul', 'meta_title' => 'H3K4me3 peptide', 'meta_keywords' => '', 'meta_description' => 'H3K4me3 peptide', 'modified' => '2015-07-17 17:41:33', 'created' => '2015-06-29 14:08:20', 'locale' => 'jpn' ), 'Antibody' => array( 'host' => '*****', 'id' => null, 'name' => null, 'description' => null, 'clonality' => null, 'isotype' => null, 'lot' => null, 'concentration' => null, 'reactivity' => null, 'type' => null, 'purity' => null, 'classification' => null, 'application_table' => null, 'storage_conditions' => null, 'storage_buffer' => null, 'precautions' => null, 'uniprot_acc' => null, 'slug' => null, 'meta_keywords' => null, 'meta_description' => null, 'modified' => null, 'created' => null, 'select_label' => null ), 'Slave' => array(), 'Group' => array(), 'Related' => array(), 'Application' => array(), 'Category' => array( (int) 0 => array( 'id' => '93', 'position' => '3', 'parent_id' => '36', 'name' => 'Peptides', 'description' => '', 'no_promo' => false, 'in_menu' => true, 'online' => true, 'tabular' => true, 'hide' => false, 'all_format' => false, 'is_antibody' => false, 'slug' => 'peptides', 'cookies_tag_id' => null, 'meta_keywords' => 'Peptides ,Proteins ', 'meta_description' => 'Diagenode offers wide range of Peptides ', 'meta_title' => 'Peptides & Proteins | Diagenode', 'modified' => '2016-01-21 15:58:23', 'created' => '2015-09-21 14:44:25', 'ProductsCategory' => array( [maximum depth reached] ), 'CookiesTag' => array([maximum depth reached]) ) ), 'Document' => array( (int) 0 => array( 'id' => '208', 'name' => 'Datasheet H3K4me3 sp003', 'description' => 'Datasheet description', 'image_id' => null, 'type' => 'Datasheet', 'url' => 'files/products/reagents/peptides/Datasheet_H3K4me3_sp003.pdf', 'slug' => 'datasheet-h3k4me3-sp003', 'meta_keywords' => null, 'meta_description' => null, 'modified' => '2015-07-07 11:47:43', 'created' => '2015-07-07 11:47:43', 'ProductsDocument' => array( [maximum depth reached] ) ), (int) 1 => array( 'id' => '725', 'name' => 'Datasheet H3K4me3 C15410003', 'description' => '<p>Datasheet description</p>', 'image_id' => null, 'type' => 'Datasheet', 'url' => 'files/products/antibodies/Datasheet_H3K4me3_C15410003.pdf', 'slug' => 'datasheet-h3k4me3-C15410003', 'meta_keywords' => '', 'meta_description' => '', 'modified' => '2015-11-20 17:39:34', 'created' => '2015-07-07 11:47:44', 'ProductsDocument' => array( [maximum depth reached] ) ) ), 'Feature' => array(), 'Image' => array(), 'Promotion' => array(), 'Protocol' => array(), 'Publication' => array( (int) 0 => array( 'id' => '4510', 'name' => 'Single amino-acid mutation in a Drosoph ila melanogaster ribosomalprotein: An insight in uL11 transcriptional activity.', 'authors' => 'Grunchec H. et al.', 'description' => '<p>The ribosomal protein uL11 is located at the basis of the ribosome P-stalk and plays a paramount role in translational efficiency. In addition, no mutant for uL11 is available suggesting that this gene is haplo-insufficient as many other Ribosomal Protein Genes (RPGs). We have previously shown that overexpression of Drosophila melanogaster uL11 enhances the transcription of many RPGs and Ribosomal Biogenesis genes (RiBis) suggesting that uL11 might globally regulate the level of translation through its transcriptional activity. Moreover, uL11 trimethylated on lysine 3 (uL11K3me3) interacts with the chromodomain of the Enhancer of Polycomb and Trithorax Corto, and both proteins co-localize with RNA Polymerase II at many sites on polytene chromosomes. These data have led to the hypothesis that the N-terminal end of uL11, and more particularly the trimethylation of lysine 3, supports the extra-ribosomal activity of uL11 in transcription. To address this question, we mutated the lysine 3 codon using a CRISPR/Cas9 strategy and obtained several lysine 3 mutants. We describe here the first mutants of D. melanogaster uL11. Unexpectedly, the uL11K3A mutant, in which the lysine 3 codon is replaced by an alanine, displays a genuine Minute phenotype known to be characteristic of RPG deletions (longer development, low fertility, high lethality, thin and short bristles) whereas the uL11K3Y mutant, in which the lysine 3 codon is replaced by a tyrosine, is unaffected. In agreement, the rate of translation decreases in uL11K3A but not in uL11K3Y. Co-immunoprecipitation experiments show that the interaction between uL11 and the Corto chromodomain is impaired by both mutations. However, Histone Association Assays indicate that the mutant proteins still bind chromatin. RNA-seq analyses from wing imaginal discs show that Corto represses RPG expression whereas very few genes are deregulated in uL11 mutants. We propose that Corto, by repressing RPG expression, ensures that all ribosomal proteins are present at the correct stoichiometry, and that uL11 fine-tunes its transcriptional regulation of RPGs.</p>', 'date' => '2022-01-01', 'pmid' => 'https://pubmed.ncbi.nlm.nih.gov/35981051/', 'doi' => '10.1371/journal.pone.0273198', 'modified' => '2022-11-21 10:40:47', 'created' => '2022-11-15 09:26:20', 'ProductsPublication' => array( [maximum depth reached] ) ) ), 'Testimonial' => array(), 'Area' => array(), 'SafetySheet' => array() ) $country = 'US' $countries_allowed = array( (int) 0 => 'CA', (int) 1 => 'US', (int) 2 => 'IE', (int) 3 => 'GB', (int) 4 => 'DK', (int) 5 => 'NO', (int) 6 => 'SE', (int) 7 => 'FI', (int) 8 => 'NL', (int) 9 => 'BE', (int) 10 => 'LU', (int) 11 => 'FR', (int) 12 => 'DE', (int) 13 => 'CH', (int) 14 => 'AT', (int) 15 => 'ES', (int) 16 => 'IT', (int) 17 => 'PT' ) $outsource = false $other_formats = array() $edit = '' $testimonials = '' $featured_testimonials = '' $related_products = '' $rrbs_service = array( (int) 0 => (int) 1894, (int) 1 => (int) 1895 ) $chipseq_service = array( (int) 0 => (int) 2683, (int) 1 => (int) 1835, (int) 2 => (int) 1836, (int) 3 => (int) 2684, (int) 4 => (int) 1838, (int) 5 => (int) 1839, (int) 6 => (int) 1856 ) $labelize = object(Closure) { } $old_catalog_number = '<br/><small><span style="color:#CCC">(sp-003-050)</span></small>' $country_code = 'US' $img = 'banners/banner-cut_tag-chipmentation-500.jpg' $label = '<img src="/img/banners/banner-customizer-back.png" alt=""/>' $document = array( 'id' => '725', 'name' => 'Datasheet H3K4me3 C15410003', 'description' => '<p>Datasheet description</p>', 'image_id' => null, 'type' => 'Datasheet', 'url' => 'files/products/antibodies/Datasheet_H3K4me3_C15410003.pdf', 'slug' => 'datasheet-h3k4me3-C15410003', 'meta_keywords' => '', 'meta_description' => '', 'modified' => '2015-11-20 17:39:34', 'created' => '2015-07-07 11:47:44', 'ProductsDocument' => array( 'id' => '409', 'product_id' => '2435', 'document_id' => '725' ) ) $publication = array( 'id' => '4510', 'name' => 'Single amino-acid mutation in a Drosoph ila melanogaster ribosomalprotein: An insight in uL11 transcriptional activity.', 'authors' => 'Grunchec H. et al.', 'description' => '<p>The ribosomal protein uL11 is located at the basis of the ribosome P-stalk and plays a paramount role in translational efficiency. In addition, no mutant for uL11 is available suggesting that this gene is haplo-insufficient as many other Ribosomal Protein Genes (RPGs). We have previously shown that overexpression of Drosophila melanogaster uL11 enhances the transcription of many RPGs and Ribosomal Biogenesis genes (RiBis) suggesting that uL11 might globally regulate the level of translation through its transcriptional activity. Moreover, uL11 trimethylated on lysine 3 (uL11K3me3) interacts with the chromodomain of the Enhancer of Polycomb and Trithorax Corto, and both proteins co-localize with RNA Polymerase II at many sites on polytene chromosomes. These data have led to the hypothesis that the N-terminal end of uL11, and more particularly the trimethylation of lysine 3, supports the extra-ribosomal activity of uL11 in transcription. To address this question, we mutated the lysine 3 codon using a CRISPR/Cas9 strategy and obtained several lysine 3 mutants. We describe here the first mutants of D. melanogaster uL11. Unexpectedly, the uL11K3A mutant, in which the lysine 3 codon is replaced by an alanine, displays a genuine Minute phenotype known to be characteristic of RPG deletions (longer development, low fertility, high lethality, thin and short bristles) whereas the uL11K3Y mutant, in which the lysine 3 codon is replaced by a tyrosine, is unaffected. In agreement, the rate of translation decreases in uL11K3A but not in uL11K3Y. Co-immunoprecipitation experiments show that the interaction between uL11 and the Corto chromodomain is impaired by both mutations. However, Histone Association Assays indicate that the mutant proteins still bind chromatin. RNA-seq analyses from wing imaginal discs show that Corto represses RPG expression whereas very few genes are deregulated in uL11 mutants. We propose that Corto, by repressing RPG expression, ensures that all ribosomal proteins are present at the correct stoichiometry, and that uL11 fine-tunes its transcriptional regulation of RPGs.</p>', 'date' => '2022-01-01', 'pmid' => 'https://pubmed.ncbi.nlm.nih.gov/35981051/', 'doi' => '10.1371/journal.pone.0273198', 'modified' => '2022-11-21 10:40:47', 'created' => '2022-11-15 09:26:20', 'ProductsPublication' => array( 'id' => '6334', 'product_id' => '2435', 'publication_id' => '4510' ) ) $externalLink = ' <a href="https://pubmed.ncbi.nlm.nih.gov/35981051/" target="_blank"><i class="fa fa-external-link"></i></a>'include - APP/View/Products/view.ctp, line 755 View::_evaluate() - CORE/Cake/View/View.php, line 971 View::_render() - CORE/Cake/View/View.php, line 933 View::render() - CORE/Cake/View/View.php, line 473 Controller::render() - CORE/Cake/Controller/Controller.php, line 963 ProductsController::slug() - APP/Controller/ProductsController.php, line 1052 ReflectionMethod::invokeArgs() - [internal], line ?? Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491 Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193 Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167 [main] - APP/webroot/index.php, line 118
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