A novel conserved RNA-binding domain protein, RBD-1, is essential for ribosome biogenesis
Synthesis of the ribosomal subunits from pre-rRNA requires a large number of trans-acting proteins and small nucleolar ribonucleoprotein particles to execute base modifications, RNA cleavages, and structural rearrangements. We have characterized a novel protein, RNA-binding domain-1 (RBD-1), that is...
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| Veröffentlicht in: | Molecular biology of the cell 2002-10, Vol.13 (10), p.3683-3695 |
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| creator | Björk, Petra Baurén, Göran Jin, ShaoBo Tong, Yong-Guang Bürglin, Thomas R Hellman, Ulf Wieslander, Lars |
| description | Synthesis of the ribosomal subunits from pre-rRNA requires a large number of trans-acting proteins and small nucleolar ribonucleoprotein particles to execute base modifications, RNA cleavages, and structural rearrangements. We have characterized a novel protein, RNA-binding domain-1 (RBD-1), that is involved in ribosome biogenesis. This protein contains six consensus RNA-binding domains and is conserved as to sequence, domain organization, and cellular location from yeast to human. RBD-1 is essential in Caenorhabditis elegans. In the dipteran Chironomus tentans, RBD-1 (Ct-RBD-1) binds pre-rRNA in vitro and anti-Ct-RBD-1 antibodies repress pre-rRNA processing in vivo. Ct-RBD-1 is mainly located in the nucleolus in an RNA polymerase I transcription-dependent manner, but it is also present in discrete foci in the interchromatin and in the cytoplasm. In cytoplasmic extracts, 20-30% of Ct-RBD-1 is associated with ribosomes and, preferentially, with the 40S ribosomal subunit. Our data suggest that RBD-1 plays a role in structurally coordinating pre-rRNA during ribosome biogenesis and that this function is conserved in all eukaryotes. |
| doi_str_mv | 10.1091/mbc.E02-03-0138 |
| format | Article |
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We have characterized a novel protein, RNA-binding domain-1 (RBD-1), that is involved in ribosome biogenesis. This protein contains six consensus RNA-binding domains and is conserved as to sequence, domain organization, and cellular location from yeast to human. RBD-1 is essential in Caenorhabditis elegans. In the dipteran Chironomus tentans, RBD-1 (Ct-RBD-1) binds pre-rRNA in vitro and anti-Ct-RBD-1 antibodies repress pre-rRNA processing in vivo. Ct-RBD-1 is mainly located in the nucleolus in an RNA polymerase I transcription-dependent manner, but it is also present in discrete foci in the interchromatin and in the cytoplasm. In cytoplasmic extracts, 20-30% of Ct-RBD-1 is associated with ribosomes and, preferentially, with the 40S ribosomal subunit. 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We have characterized a novel protein, RNA-binding domain-1 (RBD-1), that is involved in ribosome biogenesis. This protein contains six consensus RNA-binding domains and is conserved as to sequence, domain organization, and cellular location from yeast to human. RBD-1 is essential in Caenorhabditis elegans. In the dipteran Chironomus tentans, RBD-1 (Ct-RBD-1) binds pre-rRNA in vitro and anti-Ct-RBD-1 antibodies repress pre-rRNA processing in vivo. Ct-RBD-1 is mainly located in the nucleolus in an RNA polymerase I transcription-dependent manner, but it is also present in discrete foci in the interchromatin and in the cytoplasm. In cytoplasmic extracts, 20-30% of Ct-RBD-1 is associated with ribosomes and, preferentially, with the 40S ribosomal subunit. 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Baurén, Göran ; Jin, ShaoBo ; Tong, Yong-Guang ; Bürglin, Thomas R ; Hellman, Ulf ; Wieslander, Lars</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c691t-6b2d4c9384ae895109f8c008d04a22e934cdce4ad08407b050372615ebaff14c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans - metabolism</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - metabolism</topic><topic>Caenorhabditis elegans Proteins/genetics/metabolism</topic><topic>Caenorhabditis elegans/genetics/metabolism</topic><topic>Cell Nucleolus - metabolism</topic><topic>Chironomidae - anatomy & histology</topic><topic>Chironomidae - genetics</topic><topic>Chironomidae - metabolism</topic><topic>Chironomidae/anatomy & histology/genetics/metabolism</topic><topic>Chironomus tentans</topic><topic>Consensus Sequence</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungal Proteins/genetics/metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Insect Proteins/genetics/metabolism</topic><topic>Medicin och hälsovetenskap</topic><topic>Mitosis - physiology</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Nuclear Proteins/genetics/metabolism</topic><topic>Protein Structure, Tertiary</topic><topic>Ribonucleoproteins - metabolism</topic><topic>Ribosomes - metabolism</topic><topic>RNA Interference</topic><topic>RNA Polymerase I - metabolism</topic><topic>RNA Processing, Post-Transcriptional</topic><topic>RNA, Ribosomal - metabolism</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>RNA-Binding Proteins/genetics/metabolism</topic><topic>Salivary Glands - cytology</topic><topic>Salivary Glands - metabolism</topic><topic>Salivary Glands/cytology/metabolism</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Björk, Petra</creatorcontrib><creatorcontrib>Baurén, Göran</creatorcontrib><creatorcontrib>Jin, ShaoBo</creatorcontrib><creatorcontrib>Tong, Yong-Guang</creatorcontrib><creatorcontrib>Bürglin, Thomas R</creatorcontrib><creatorcontrib>Hellman, Ulf</creatorcontrib><creatorcontrib>Wieslander, Lars</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Södertörns högskola- SwePub</collection><collection>SWEPUB Stockholms universitet</collection><collection>SWEPUB Uppsala universitet</collection><collection>SWEPUB Freely available online</collection><collection>SwePub Articles full text</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Björk, Petra</au><au>Baurén, Göran</au><au>Jin, ShaoBo</au><au>Tong, Yong-Guang</au><au>Bürglin, Thomas R</au><au>Hellman, Ulf</au><au>Wieslander, Lars</au><au>Gall, Joseph</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel conserved RNA-binding domain protein, RBD-1, is essential for ribosome biogenesis</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2002-10-01</date><risdate>2002</risdate><volume>13</volume><issue>10</issue><spage>3683</spage><epage>3695</epage><pages>3683-3695</pages><issn>1059-1524</issn><issn>1939-4586</issn><eissn>1939-4586</eissn><abstract>Synthesis of the ribosomal subunits from pre-rRNA requires a large number of trans-acting proteins and small nucleolar ribonucleoprotein particles to execute base modifications, RNA cleavages, and structural rearrangements. We have characterized a novel protein, RNA-binding domain-1 (RBD-1), that is involved in ribosome biogenesis. This protein contains six consensus RNA-binding domains and is conserved as to sequence, domain organization, and cellular location from yeast to human. RBD-1 is essential in Caenorhabditis elegans. In the dipteran Chironomus tentans, RBD-1 (Ct-RBD-1) binds pre-rRNA in vitro and anti-Ct-RBD-1 antibodies repress pre-rRNA processing in vivo. Ct-RBD-1 is mainly located in the nucleolus in an RNA polymerase I transcription-dependent manner, but it is also present in discrete foci in the interchromatin and in the cytoplasm. In cytoplasmic extracts, 20-30% of Ct-RBD-1 is associated with ribosomes and, preferentially, with the 40S ribosomal subunit. 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| subjects | Animals Caenorhabditis elegans Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism Caenorhabditis elegans Proteins/genetics/metabolism Caenorhabditis elegans/genetics/metabolism Cell Nucleolus - metabolism Chironomidae - anatomy & histology Chironomidae - genetics Chironomidae - metabolism Chironomidae/anatomy & histology/genetics/metabolism Chironomus tentans Consensus Sequence Fungal Proteins - genetics Fungal Proteins - metabolism Fungal Proteins/genetics/metabolism HeLa Cells Humans Insect Proteins - genetics Insect Proteins - metabolism Insect Proteins/genetics/metabolism Medicin och hälsovetenskap Mitosis - physiology Nuclear Proteins - genetics Nuclear Proteins - metabolism Nuclear Proteins/genetics/metabolism Protein Structure, Tertiary Ribonucleoproteins - metabolism Ribosomes - metabolism RNA Interference RNA Polymerase I - metabolism RNA Processing, Post-Transcriptional RNA, Ribosomal - metabolism RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism RNA-Binding Proteins/genetics/metabolism Salivary Glands - cytology Salivary Glands - metabolism Salivary Glands/cytology/metabolism Transcription, Genetic |
| title | A novel conserved RNA-binding domain protein, RBD-1, is essential for ribosome biogenesis |
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