Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules

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Cytoplasmic events depending on RNA-binding proteins contribute to the fine-tuning of gene expression. Sterile α motif-containing RNA-binding proteins constitute a novel family of post-transcriptional regulators that recognize a specific RNA sequence motif known as Smaug recognition element (SRE). T...

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Autores principales:	Baez, M.V., Boccaccio, G.L.
Formato:	Artículo publishedVersion
Publicado:	2005
Materias:	Degradation Genes Proteins RNA Deadenylation Gene expression RNA-binding proteins Cytology messenger RNA protein mSmaug 1 protein Smaug protein Staufen protein TIA 1 protein TIAR repressor protein RNA binding protein unclassified drug animal cell article cell granule central nervous system chromosome 14 cytoplasm Drosophila fibroblast gene expression genome human human cell molecular recognition nonhuman nucleotide sequence priority journal protein degradation protein expression protein family reporter gene RNA sequence RNA translation stress synapse synaptosome translation regulation translation repression Amino Acid Motifs Animals Blotting, Western Cell Line Central Nervous System Cercopithecus aethiops Chromosomes, Human, Pair 14 COS Cells Cricetinae Cytoplasm Cytoplasmic Granules DNA, Complementary Drosophila Proteins Fibroblasts Gene Library Hela Cells Humans Luciferases Mice Microscopy, Confocal Microscopy, Fluorescence Models, Genetic Molecular Sequence Data Neurons Plasmids Polyribosomes Protein Binding Protein Biosynthesis Repressor Proteins Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger RNA-Binding Proteins Synapses Tissue Distribution Transfection Animalia Mammalia Murinae
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00219258_v280_n52_p43131_Baez https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00219258_v280_n52_p43131_Baez_oai
Aporte de:	Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires

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spelling	I28-R145-paper_00219258_v280_n52_p43131_Baez_oai2024-08-16 Baez, M.V. Boccaccio, G.L. 2005 Cytoplasmic events depending on RNA-binding proteins contribute to the fine-tuning of gene expression. Sterile α motif-containing RNA-binding proteins constitute a novel family of post-transcriptional regulators that recognize a specific RNA sequence motif known as Smaug recognition element (SRE). The Drosophila member of this family, dSmaug, triggers the translational repression and deadenylation of maternal mRNAs by independent mechanisms, and the yeast homologue Vts1 stimulates degradation of SRE-containing messengers. Two homologous genes are present in the mammalian genome. Here we showed that hSmaug 1, encoded in human chromosome 14, represses the translation of reporter transcripts carrying SRE motifs. When expressed in fibroblasts, hSmaug 1 forms cytoplasmic granules that contain polyadenylated mRNA and the RNA-binding proteins Staufen, TIAR, TIA-1, and HuR. Smaug 1 foci are distinct from degradation foci. The murine protein mSmaug 1 is expressed in the central nervous system and is abundant in post-synaptic densities, a subcellular region where translation is tightly regulated by synaptic stimulation. Biochemical analysis indicated that mSmaug 1 is present in synaptoneurosomal 20 S particles. These results suggest a role for mammalian Smaug 1 in RNA granule formation and translation regulation in neurons. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc. Fil:Baez, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Boccaccio, G.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. application/pdf http://hdl.handle.net/20.500.12110/paper_00219258_v280_n52_p43131_Baez info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar J. Biol. Chem. 2005;280(52):43131-43140 Degradation Genes Proteins RNA Deadenylation Gene expression RNA-binding proteins Cytology messenger RNA protein mSmaug 1 protein Smaug protein Staufen protein TIA 1 protein TIAR repressor protein RNA binding protein unclassified drug animal cell article cell granule central nervous system chromosome 14 cytoplasm Drosophila fibroblast gene expression genome human human cell molecular recognition nonhuman nucleotide sequence priority journal protein degradation protein expression protein family reporter gene RNA sequence RNA translation stress synapse synaptosome translation regulation translation repression Amino Acid Motifs Animals Blotting, Western Cell Line Central Nervous System Cercopithecus aethiops Chromosomes, Human, Pair 14 COS Cells Cricetinae Cytoplasm Cytoplasmic Granules DNA, Complementary Drosophila Drosophila Proteins Fibroblasts Gene Library Hela Cells Humans Luciferases Mice Microscopy, Confocal Microscopy, Fluorescence Models, Genetic Molecular Sequence Data Neurons Plasmids Polyribosomes Protein Binding Protein Biosynthesis Repressor Proteins Reverse Transcriptase Polymerase Chain Reaction RNA RNA, Messenger RNA-Binding Proteins Synapses Tissue Distribution Transfection Animalia Mammalia Murinae Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00219258_v280_n52_p43131_Baez_oai
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-145
collection	Repositorio Digital de la Universidad de Buenos Aires (UBA)
topic	Degradation Genes Proteins RNA Deadenylation Gene expression RNA-binding proteins Cytology messenger RNA protein mSmaug 1 protein Smaug protein Staufen protein TIA 1 protein TIAR repressor protein RNA binding protein unclassified drug animal cell article cell granule central nervous system chromosome 14 cytoplasm Drosophila fibroblast gene expression genome human human cell molecular recognition nonhuman nucleotide sequence priority journal protein degradation protein expression protein family reporter gene RNA sequence RNA translation stress synapse synaptosome translation regulation translation repression Amino Acid Motifs Animals Blotting, Western Cell Line Central Nervous System Cercopithecus aethiops Chromosomes, Human, Pair 14 COS Cells Cricetinae Cytoplasm Cytoplasmic Granules DNA, Complementary Drosophila Drosophila Proteins Fibroblasts Gene Library Hela Cells Humans Luciferases Mice Microscopy, Confocal Microscopy, Fluorescence Models, Genetic Molecular Sequence Data Neurons Plasmids Polyribosomes Protein Binding Protein Biosynthesis Repressor Proteins Reverse Transcriptase Polymerase Chain Reaction RNA RNA, Messenger RNA-Binding Proteins Synapses Tissue Distribution Transfection Animalia Mammalia Murinae
spellingShingle	Degradation Genes Proteins RNA Deadenylation Gene expression RNA-binding proteins Cytology messenger RNA protein mSmaug 1 protein Smaug protein Staufen protein TIA 1 protein TIAR repressor protein RNA binding protein unclassified drug animal cell article cell granule central nervous system chromosome 14 cytoplasm Drosophila fibroblast gene expression genome human human cell molecular recognition nonhuman nucleotide sequence priority journal protein degradation protein expression protein family reporter gene RNA sequence RNA translation stress synapse synaptosome translation regulation translation repression Amino Acid Motifs Animals Blotting, Western Cell Line Central Nervous System Cercopithecus aethiops Chromosomes, Human, Pair 14 COS Cells Cricetinae Cytoplasm Cytoplasmic Granules DNA, Complementary Drosophila Drosophila Proteins Fibroblasts Gene Library Hela Cells Humans Luciferases Mice Microscopy, Confocal Microscopy, Fluorescence Models, Genetic Molecular Sequence Data Neurons Plasmids Polyribosomes Protein Binding Protein Biosynthesis Repressor Proteins Reverse Transcriptase Polymerase Chain Reaction RNA RNA, Messenger RNA-Binding Proteins Synapses Tissue Distribution Transfection Animalia Mammalia Murinae Baez, M.V. Boccaccio, G.L. Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
topic_facet	Degradation Genes Proteins RNA Deadenylation Gene expression RNA-binding proteins Cytology messenger RNA protein mSmaug 1 protein Smaug protein Staufen protein TIA 1 protein TIAR repressor protein RNA binding protein unclassified drug animal cell article cell granule central nervous system chromosome 14 cytoplasm Drosophila fibroblast gene expression genome human human cell molecular recognition nonhuman nucleotide sequence priority journal protein degradation protein expression protein family reporter gene RNA sequence RNA translation stress synapse synaptosome translation regulation translation repression Amino Acid Motifs Animals Blotting, Western Cell Line Central Nervous System Cercopithecus aethiops Chromosomes, Human, Pair 14 COS Cells Cricetinae Cytoplasm Cytoplasmic Granules DNA, Complementary Drosophila Drosophila Proteins Fibroblasts Gene Library Hela Cells Humans Luciferases Mice Microscopy, Confocal Microscopy, Fluorescence Models, Genetic Molecular Sequence Data Neurons Plasmids Polyribosomes Protein Binding Protein Biosynthesis Repressor Proteins Reverse Transcriptase Polymerase Chain Reaction RNA RNA, Messenger RNA-Binding Proteins Synapses Tissue Distribution Transfection Animalia Mammalia Murinae
description	Cytoplasmic events depending on RNA-binding proteins contribute to the fine-tuning of gene expression. Sterile α motif-containing RNA-binding proteins constitute a novel family of post-transcriptional regulators that recognize a specific RNA sequence motif known as Smaug recognition element (SRE). The Drosophila member of this family, dSmaug, triggers the translational repression and deadenylation of maternal mRNAs by independent mechanisms, and the yeast homologue Vts1 stimulates degradation of SRE-containing messengers. Two homologous genes are present in the mammalian genome. Here we showed that hSmaug 1, encoded in human chromosome 14, represses the translation of reporter transcripts carrying SRE motifs. When expressed in fibroblasts, hSmaug 1 forms cytoplasmic granules that contain polyadenylated mRNA and the RNA-binding proteins Staufen, TIAR, TIA-1, and HuR. Smaug 1 foci are distinct from degradation foci. The murine protein mSmaug 1 is expressed in the central nervous system and is abundant in post-synaptic densities, a subcellular region where translation is tightly regulated by synaptic stimulation. Biochemical analysis indicated that mSmaug 1 is present in synaptoneurosomal 20 S particles. These results suggest a role for mammalian Smaug 1 in RNA granule formation and translation regulation in neurons. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
format	Artículo Artículo publishedVersion
author	Baez, M.V. Boccaccio, G.L.
author_facet	Baez, M.V. Boccaccio, G.L.
author_sort	Baez, M.V.
title	Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title_short	Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title_full	Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title_fullStr	Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title_full_unstemmed	Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title_sort	mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
publishDate	2005
url	http://hdl.handle.net/20.500.12110/paper_00219258_v280_n52_p43131_Baez https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00219258_v280_n52_p43131_Baez_oai
work_keys_str_mv	AT baezmv mammaliansmaugisatranslationalrepressorthatformscytoplasmicfocisimilartostressgranules AT boccacciogl mammaliansmaugisatranslationalrepressorthatformscytoplasmicfocisimilartostressgranules
_version_	1809356871833747456

Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules

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