A novel GTPase activated by the small subunit of ribosome
The GTPase activity of Escherichia coli YjeQ, here named RsgA (ribosome small subunit-dependent GTPase A), has been shown to be significantly enhanced by ribosome or its small subunit. The enhancement of GTPase activity was inhibited by several aminoglycosides bound at the A site of the small subuni...
Gespeichert in:
| Veröffentlicht in: | Nucleic acids research 2004-01, Vol.32 (17), p.5303-5309 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 5309 |
|---|---|
| container_issue | 17 |
| container_start_page | 5303 |
| container_title | Nucleic acids research |
| container_volume | 32 |
| creator | Himeno, Hyouta Hanawa-Suetsugu, Kyoko Kimura, Takatsugu Takagi, Kuniaki Sugiyama, Wakana Shirata, Shinobu Mikami, Tomoyuki Odagiri, Fujiko Osanai, Yukiko Watanabe, Daisuke Goto, Simon Kalachnyuk, Liliya Ushida, Chisato Muto, Akira |
| description | The GTPase activity of Escherichia coli YjeQ, here named RsgA (ribosome small subunit-dependent GTPase A), has been shown to be significantly enhanced by ribosome or its small subunit. The enhancement of GTPase activity was inhibited by several aminoglycosides bound at the A site of the small subunit, but not by a P site-specific antibiotic. RsgA stably bound the small subunit in the presence of GDPNP, but not in the presence of GTP or GDP, to dissociate ribosome into subunits. Disruption of the gene for RsgA from the genome affected the growth of the cells, which predominantly contained the dissociated subunits having only a weak activation activity of RsgA. We also found that 17S RNA, a putative precursor of 16S rRNA, was contained in the small subunit of the ribosome from the RsgA-deletion strain. RsgA is a novel GTPase that might provide a new insight into the function of ribosome. |
| doi_str_mv | 10.1093/nar/gkh861 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_521671</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>729725871</sourcerecordid><originalsourceid>FETCH-LOGICAL-c566t-d4d24e2af5b5099ec2bfafc4895ce41f100ec68859a78f44953c23f1f01ac58f3</originalsourceid><addsrcrecordid>eNqN0c9rFDEUB_Agil2rF_8ACR48FMa-l18zOXgoS38IBUUqSC8hk026085MajKztP-9kV3a6kUvyeF9XsJ7X0LeInxE0PxwtOnw6mbdKHxGFsgVq4RW7DlZAAdZIYhmj7zK-RoABUrxkuyVUymp1YLoIzrGje_p6cVXmz21buo2dvIr2t7Tae1pHmzf0zy389hNNAaaujbmOPjX5EWwffZvdvc--X5yfLE8q86_nH5eHp1XTio1VSuxYsIzG2QrQWvvWBtscKLR0nmBAQG8U00jta2bIISW3DEeMABaJ5vA98mn7bu3czv4lfPjlGxvblM32HRvou3Mn5WxW5uruDGSoaqx9H_Y9af4c_Z5MkOXne97O_o4Z6NU-VJD80-IutYSgf8HVKqMJwp8_xe8jnMay7YMA1A108AKOtgil2LOyYeH0RDM73xNydds8y343dNlPNJdoAVUW9Dlyd891G26MarmtTRnPy6N-FYDssulkfwXEq-wEg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>200672902</pqid></control><display><type>article</type><title>A novel GTPase activated by the small subunit of ribosome</title><source>MEDLINE</source><source>Oxford Journals Open Access Collection</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Himeno, Hyouta ; Hanawa-Suetsugu, Kyoko ; Kimura, Takatsugu ; Takagi, Kuniaki ; Sugiyama, Wakana ; Shirata, Shinobu ; Mikami, Tomoyuki ; Odagiri, Fujiko ; Osanai, Yukiko ; Watanabe, Daisuke ; Goto, Simon ; Kalachnyuk, Liliya ; Ushida, Chisato ; Muto, Akira</creator><creatorcontrib>Himeno, Hyouta ; Hanawa-Suetsugu, Kyoko ; Kimura, Takatsugu ; Takagi, Kuniaki ; Sugiyama, Wakana ; Shirata, Shinobu ; Mikami, Tomoyuki ; Odagiri, Fujiko ; Osanai, Yukiko ; Watanabe, Daisuke ; Goto, Simon ; Kalachnyuk, Liliya ; Ushida, Chisato ; Muto, Akira</creatorcontrib><description>The GTPase activity of Escherichia coli YjeQ, here named RsgA (ribosome small subunit-dependent GTPase A), has been shown to be significantly enhanced by ribosome or its small subunit. The enhancement of GTPase activity was inhibited by several aminoglycosides bound at the A site of the small subunit, but not by a P site-specific antibiotic. RsgA stably bound the small subunit in the presence of GDPNP, but not in the presence of GTP or GDP, to dissociate ribosome into subunits. Disruption of the gene for RsgA from the genome affected the growth of the cells, which predominantly contained the dissociated subunits having only a weak activation activity of RsgA. We also found that 17S RNA, a putative precursor of 16S rRNA, was contained in the small subunit of the ribosome from the RsgA-deletion strain. RsgA is a novel GTPase that might provide a new insight into the function of ribosome.</description><identifier>ISSN: 0305-1048</identifier><identifier>ISSN: 1362-4962</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/gkh861</identifier><identifier>PMID: 15466596</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Anti-Bacterial Agents - pharmacology ; Enzyme Activation ; Escherichia coli ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; GTP Phosphohydrolases - genetics ; GTP Phosphohydrolases - metabolism ; Guanine Nucleotides - metabolism ; Mutation ; Ribosomes - chemistry ; Ribosomes - drug effects ; Ribosomes - metabolism</subject><ispartof>Nucleic acids research, 2004-01, Vol.32 (17), p.5303-5309</ispartof><rights>Copyright Oxford University Press(England) 2004</rights><rights>Copyright © 2004 Oxford University Press 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c566t-d4d24e2af5b5099ec2bfafc4895ce41f100ec68859a78f44953c23f1f01ac58f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC521671/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC521671/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15466596$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Himeno, Hyouta</creatorcontrib><creatorcontrib>Hanawa-Suetsugu, Kyoko</creatorcontrib><creatorcontrib>Kimura, Takatsugu</creatorcontrib><creatorcontrib>Takagi, Kuniaki</creatorcontrib><creatorcontrib>Sugiyama, Wakana</creatorcontrib><creatorcontrib>Shirata, Shinobu</creatorcontrib><creatorcontrib>Mikami, Tomoyuki</creatorcontrib><creatorcontrib>Odagiri, Fujiko</creatorcontrib><creatorcontrib>Osanai, Yukiko</creatorcontrib><creatorcontrib>Watanabe, Daisuke</creatorcontrib><creatorcontrib>Goto, Simon</creatorcontrib><creatorcontrib>Kalachnyuk, Liliya</creatorcontrib><creatorcontrib>Ushida, Chisato</creatorcontrib><creatorcontrib>Muto, Akira</creatorcontrib><title>A novel GTPase activated by the small subunit of ribosome</title><title>Nucleic acids research</title><addtitle>Nucl. Acids Res</addtitle><description>The GTPase activity of Escherichia coli YjeQ, here named RsgA (ribosome small subunit-dependent GTPase A), has been shown to be significantly enhanced by ribosome or its small subunit. The enhancement of GTPase activity was inhibited by several aminoglycosides bound at the A site of the small subunit, but not by a P site-specific antibiotic. RsgA stably bound the small subunit in the presence of GDPNP, but not in the presence of GTP or GDP, to dissociate ribosome into subunits. Disruption of the gene for RsgA from the genome affected the growth of the cells, which predominantly contained the dissociated subunits having only a weak activation activity of RsgA. We also found that 17S RNA, a putative precursor of 16S rRNA, was contained in the small subunit of the ribosome from the RsgA-deletion strain. RsgA is a novel GTPase that might provide a new insight into the function of ribosome.</description><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Enzyme Activation</subject><subject>Escherichia coli</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>GTP Phosphohydrolases - genetics</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>Guanine Nucleotides - metabolism</subject><subject>Mutation</subject><subject>Ribosomes - chemistry</subject><subject>Ribosomes - drug effects</subject><subject>Ribosomes - metabolism</subject><issn>0305-1048</issn><issn>1362-4962</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0c9rFDEUB_Agil2rF_8ACR48FMa-l18zOXgoS38IBUUqSC8hk026085MajKztP-9kV3a6kUvyeF9XsJ7X0LeInxE0PxwtOnw6mbdKHxGFsgVq4RW7DlZAAdZIYhmj7zK-RoABUrxkuyVUymp1YLoIzrGje_p6cVXmz21buo2dvIr2t7Tae1pHmzf0zy389hNNAaaujbmOPjX5EWwffZvdvc--X5yfLE8q86_nH5eHp1XTio1VSuxYsIzG2QrQWvvWBtscKLR0nmBAQG8U00jta2bIISW3DEeMABaJ5vA98mn7bu3czv4lfPjlGxvblM32HRvou3Mn5WxW5uruDGSoaqx9H_Y9af4c_Z5MkOXne97O_o4Z6NU-VJD80-IutYSgf8HVKqMJwp8_xe8jnMay7YMA1A108AKOtgil2LOyYeH0RDM73xNydds8y343dNlPNJdoAVUW9Dlyd891G26MarmtTRnPy6N-FYDssulkfwXEq-wEg</recordid><startdate>20040101</startdate><enddate>20040101</enddate><creator>Himeno, Hyouta</creator><creator>Hanawa-Suetsugu, Kyoko</creator><creator>Kimura, Takatsugu</creator><creator>Takagi, Kuniaki</creator><creator>Sugiyama, Wakana</creator><creator>Shirata, Shinobu</creator><creator>Mikami, Tomoyuki</creator><creator>Odagiri, Fujiko</creator><creator>Osanai, Yukiko</creator><creator>Watanabe, Daisuke</creator><creator>Goto, Simon</creator><creator>Kalachnyuk, Liliya</creator><creator>Ushida, Chisato</creator><creator>Muto, Akira</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20040101</creationdate><title>A novel GTPase activated by the small subunit of ribosome</title><author>Himeno, Hyouta ; Hanawa-Suetsugu, Kyoko ; Kimura, Takatsugu ; Takagi, Kuniaki ; Sugiyama, Wakana ; Shirata, Shinobu ; Mikami, Tomoyuki ; Odagiri, Fujiko ; Osanai, Yukiko ; Watanabe, Daisuke ; Goto, Simon ; Kalachnyuk, Liliya ; Ushida, Chisato ; Muto, Akira</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c566t-d4d24e2af5b5099ec2bfafc4895ce41f100ec68859a78f44953c23f1f01ac58f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Enzyme Activation</topic><topic>Escherichia coli</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>GTP Phosphohydrolases - genetics</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>Guanine Nucleotides - metabolism</topic><topic>Mutation</topic><topic>Ribosomes - chemistry</topic><topic>Ribosomes - drug effects</topic><topic>Ribosomes - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Himeno, Hyouta</creatorcontrib><creatorcontrib>Hanawa-Suetsugu, Kyoko</creatorcontrib><creatorcontrib>Kimura, Takatsugu</creatorcontrib><creatorcontrib>Takagi, Kuniaki</creatorcontrib><creatorcontrib>Sugiyama, Wakana</creatorcontrib><creatorcontrib>Shirata, Shinobu</creatorcontrib><creatorcontrib>Mikami, Tomoyuki</creatorcontrib><creatorcontrib>Odagiri, Fujiko</creatorcontrib><creatorcontrib>Osanai, Yukiko</creatorcontrib><creatorcontrib>Watanabe, Daisuke</creatorcontrib><creatorcontrib>Goto, Simon</creatorcontrib><creatorcontrib>Kalachnyuk, Liliya</creatorcontrib><creatorcontrib>Ushida, Chisato</creatorcontrib><creatorcontrib>Muto, Akira</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Himeno, Hyouta</au><au>Hanawa-Suetsugu, Kyoko</au><au>Kimura, Takatsugu</au><au>Takagi, Kuniaki</au><au>Sugiyama, Wakana</au><au>Shirata, Shinobu</au><au>Mikami, Tomoyuki</au><au>Odagiri, Fujiko</au><au>Osanai, Yukiko</au><au>Watanabe, Daisuke</au><au>Goto, Simon</au><au>Kalachnyuk, Liliya</au><au>Ushida, Chisato</au><au>Muto, Akira</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel GTPase activated by the small subunit of ribosome</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucl. Acids Res</addtitle><date>2004-01-01</date><risdate>2004</risdate><volume>32</volume><issue>17</issue><spage>5303</spage><epage>5309</epage><pages>5303-5309</pages><issn>0305-1048</issn><issn>1362-4962</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>The GTPase activity of Escherichia coli YjeQ, here named RsgA (ribosome small subunit-dependent GTPase A), has been shown to be significantly enhanced by ribosome or its small subunit. The enhancement of GTPase activity was inhibited by several aminoglycosides bound at the A site of the small subunit, but not by a P site-specific antibiotic. RsgA stably bound the small subunit in the presence of GDPNP, but not in the presence of GTP or GDP, to dissociate ribosome into subunits. Disruption of the gene for RsgA from the genome affected the growth of the cells, which predominantly contained the dissociated subunits having only a weak activation activity of RsgA. We also found that 17S RNA, a putative precursor of 16S rRNA, was contained in the small subunit of the ribosome from the RsgA-deletion strain. RsgA is a novel GTPase that might provide a new insight into the function of ribosome.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>15466596</pmid><doi>10.1093/nar/gkh861</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0305-1048 |
| ispartof | Nucleic acids research, 2004-01, Vol.32 (17), p.5303-5309 |
| issn | 0305-1048 1362-4962 1362-4962 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_521671 |
| source | MEDLINE; Oxford Journals Open Access Collection; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Anti-Bacterial Agents - pharmacology Enzyme Activation Escherichia coli Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism GTP Phosphohydrolases - genetics GTP Phosphohydrolases - metabolism Guanine Nucleotides - metabolism Mutation Ribosomes - chemistry Ribosomes - drug effects Ribosomes - metabolism |
| title | A novel GTPase activated by the small subunit of ribosome |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T01%3A25%3A29IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20novel%20GTPase%20activated%20by%20the%20small%20subunit%20of%20ribosome&rft.jtitle=Nucleic%20acids%20research&rft.au=Himeno,%20Hyouta&rft.date=2004-01-01&rft.volume=32&rft.issue=17&rft.spage=5303&rft.epage=5309&rft.pages=5303-5309&rft.issn=0305-1048&rft.eissn=1362-4962&rft.coden=NARHAD&rft_id=info:doi/10.1093/nar/gkh861&rft_dat=%3Cproquest_pubme%3E729725871%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=200672902&rft_id=info:pmid/15466596&rfr_iscdi=true |