Structure of a Beheaded 30 S Ribosomal Subunit from Thermus thermophilus
The 22S ribonucleoproten particles containing the 5′ (body) and the central (platform) domains of the Thermus thermophilus 30S subunit has been studied by sedimentation, neutron scattering and electron microscopy. The RNP particles have been obtained by oligonucleotide-directed cleavage of 16S RNA w...
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| Veröffentlicht in: | Journal of molecular biology 1999-09, Vol.292 (3), p.633-639 |
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| container_end_page | 639 |
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| container_title | Journal of molecular biology |
| container_volume | 292 |
| creator | Serdyuk, Igor Ulitin, Andrey Kolesnikov, Igor Vasiliev, Victor Aksenov, Victor Zaccai, Guiseppe Svergun, Dmitri Kozin, Michael Willumeit, Regine |
| description | The 22S ribonucleoproten particles containing the 5′ (body) and the central (platform) domains of the Thermus thermophilus 30S subunit has been studied by sedimentation, neutron scattering and electron microscopy. The RNP particles have been obtained by oligonucleotide-directed cleavage of 16S RNA with ribonulease H in the region of the 900th nucleotide of the protein-deficient derivatives of the 30S subunits. It is shown that these RNP particles are very compact, though their form and dimensions differ slightly from those expected from the electron microscopy model of the 30S subunit beheaded by computer simulation. The particles are subdivided into two structural domains whose mutual arrangement differs from that of the corresponding morphological parts of the native 30S subunit. Electron microscopy demonstrates that the mutual arrangement of domains in the RNP particles is not strictly fixed suggesting that interaction with the third domain of the 30S subunit is a requisite for their correct fitting. |
| doi_str_mv | 10.1006/jmbi.1999.3109 |
| format | Article |
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The RNP particles have been obtained by oligonucleotide-directed cleavage of 16S RNA with ribonulease H in the region of the 900th nucleotide of the protein-deficient derivatives of the 30S subunits. It is shown that these RNP particles are very compact, though their form and dimensions differ slightly from those expected from the electron microscopy model of the 30S subunit beheaded by computer simulation. The particles are subdivided into two structural domains whose mutual arrangement differs from that of the corresponding morphological parts of the native 30S subunit. Electron microscopy demonstrates that the mutual arrangement of domains in the RNP particles is not strictly fixed suggesting that interaction with the third domain of the 30S subunit is a requisite for their correct fitting.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1006/jmbi.1999.3109</identifier><identifier>PMID: 10497027</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Computer Simulation ; domain structure ; electron microscopy ; Microscopy, Electron ; neutron scattering ; Neutrons ; Ribonuclease H ; Ribonucleoproteins - chemistry ; Ribonucleoproteins - ultrastructure ; Ribosomes - chemistry ; RNP particles ; Scattering, Radiation ; Thermus thermophilus ; Thermus thermophilus - chemistry ; Ultracentrifugation</subject><ispartof>Journal of molecular biology, 1999-09, Vol.292 (3), p.633-639</ispartof><rights>1999 Academic Press</rights><rights>Copyright 1999 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/jmbi.1999.3109$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10497027$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Serdyuk, Igor</creatorcontrib><creatorcontrib>Ulitin, Andrey</creatorcontrib><creatorcontrib>Kolesnikov, Igor</creatorcontrib><creatorcontrib>Vasiliev, Victor</creatorcontrib><creatorcontrib>Aksenov, Victor</creatorcontrib><creatorcontrib>Zaccai, Guiseppe</creatorcontrib><creatorcontrib>Svergun, Dmitri</creatorcontrib><creatorcontrib>Kozin, Michael</creatorcontrib><creatorcontrib>Willumeit, Regine</creatorcontrib><title>Structure of a Beheaded 30 S Ribosomal Subunit from Thermus thermophilus</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The 22S ribonucleoproten particles containing the 5′ (body) and the central (platform) domains of the Thermus thermophilus 30S subunit has been studied by sedimentation, neutron scattering and electron microscopy. The RNP particles have been obtained by oligonucleotide-directed cleavage of 16S RNA with ribonulease H in the region of the 900th nucleotide of the protein-deficient derivatives of the 30S subunits. It is shown that these RNP particles are very compact, though their form and dimensions differ slightly from those expected from the electron microscopy model of the 30S subunit beheaded by computer simulation. The particles are subdivided into two structural domains whose mutual arrangement differs from that of the corresponding morphological parts of the native 30S subunit. Electron microscopy demonstrates that the mutual arrangement of domains in the RNP particles is not strictly fixed suggesting that interaction with the third domain of the 30S subunit is a requisite for their correct fitting.</description><subject>Computer Simulation</subject><subject>domain structure</subject><subject>electron microscopy</subject><subject>Microscopy, Electron</subject><subject>neutron scattering</subject><subject>Neutrons</subject><subject>Ribonuclease H</subject><subject>Ribonucleoproteins - chemistry</subject><subject>Ribonucleoproteins - ultrastructure</subject><subject>Ribosomes - chemistry</subject><subject>RNP particles</subject><subject>Scattering, Radiation</subject><subject>Thermus thermophilus</subject><subject>Thermus thermophilus - chemistry</subject><subject>Ultracentrifugation</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkT1PwzAQQC0EoqWwMiJPbCl2nPhjhAooUiUkWmbLTi6qq6QudozEvydRy8z0lncn3T2EbimZU0L4w66zbk6VUnNGiTpDU0qkyiRn8hxNCcnzLJeMT9BVjDtCSMkKeYkmlBRKkFxM0XLdh1T1KQD2DTb4CbZgaqgxI3iNP5z10Xemxetk0971uAm-w5sthC5F3I_0h61rU7xGF41pI9ycOEOfL8-bxTJbvb--LR5XGeRS9JkBTktrubW04ayyNmdK2KphwJrSlMxIQ-oGBrBCDSNK1EVhVCllXfBGSjZD98e9h-C_EsRedy5W0LZmDz5FLYgQRIryX5EKlvOyoIN4dxKT7aDWh-A6E37035MGQR4FGO76dhB0rBzsK6hdgKrXtXeDrMceeuyhxx567MF-AVv2fBQ</recordid><startdate>19990924</startdate><enddate>19990924</enddate><creator>Serdyuk, Igor</creator><creator>Ulitin, Andrey</creator><creator>Kolesnikov, Igor</creator><creator>Vasiliev, Victor</creator><creator>Aksenov, Victor</creator><creator>Zaccai, Guiseppe</creator><creator>Svergun, Dmitri</creator><creator>Kozin, Michael</creator><creator>Willumeit, Regine</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>7TM</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19990924</creationdate><title>Structure of a Beheaded 30 S Ribosomal Subunit from Thermus thermophilus</title><author>Serdyuk, Igor ; Ulitin, Andrey ; Kolesnikov, Igor ; Vasiliev, Victor ; Aksenov, Victor ; Zaccai, Guiseppe ; Svergun, Dmitri ; Kozin, Michael ; Willumeit, Regine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e287t-ae615bb6bb1f63cbb2397bcf3e3f5a53a8a0dfea8a349e2897d44a9588d46f883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Computer Simulation</topic><topic>domain structure</topic><topic>electron microscopy</topic><topic>Microscopy, Electron</topic><topic>neutron scattering</topic><topic>Neutrons</topic><topic>Ribonuclease H</topic><topic>Ribonucleoproteins - chemistry</topic><topic>Ribonucleoproteins - ultrastructure</topic><topic>Ribosomes - chemistry</topic><topic>RNP particles</topic><topic>Scattering, Radiation</topic><topic>Thermus thermophilus</topic><topic>Thermus thermophilus - chemistry</topic><topic>Ultracentrifugation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Serdyuk, Igor</creatorcontrib><creatorcontrib>Ulitin, Andrey</creatorcontrib><creatorcontrib>Kolesnikov, Igor</creatorcontrib><creatorcontrib>Vasiliev, Victor</creatorcontrib><creatorcontrib>Aksenov, Victor</creatorcontrib><creatorcontrib>Zaccai, Guiseppe</creatorcontrib><creatorcontrib>Svergun, Dmitri</creatorcontrib><creatorcontrib>Kozin, Michael</creatorcontrib><creatorcontrib>Willumeit, Regine</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Serdyuk, Igor</au><au>Ulitin, Andrey</au><au>Kolesnikov, Igor</au><au>Vasiliev, Victor</au><au>Aksenov, Victor</au><au>Zaccai, Guiseppe</au><au>Svergun, Dmitri</au><au>Kozin, Michael</au><au>Willumeit, Regine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of a Beheaded 30 S Ribosomal Subunit from Thermus thermophilus</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1999-09-24</date><risdate>1999</risdate><volume>292</volume><issue>3</issue><spage>633</spage><epage>639</epage><pages>633-639</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>The 22S ribonucleoproten particles containing the 5′ (body) and the central (platform) domains of the Thermus thermophilus 30S subunit has been studied by sedimentation, neutron scattering and electron microscopy. The RNP particles have been obtained by oligonucleotide-directed cleavage of 16S RNA with ribonulease H in the region of the 900th nucleotide of the protein-deficient derivatives of the 30S subunits. It is shown that these RNP particles are very compact, though their form and dimensions differ slightly from those expected from the electron microscopy model of the 30S subunit beheaded by computer simulation. The particles are subdivided into two structural domains whose mutual arrangement differs from that of the corresponding morphological parts of the native 30S subunit. Electron microscopy demonstrates that the mutual arrangement of domains in the RNP particles is not strictly fixed suggesting that interaction with the third domain of the 30S subunit is a requisite for their correct fitting.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>10497027</pmid><doi>10.1006/jmbi.1999.3109</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of molecular biology, 1999-09, Vol.292 (3), p.633-639 |
| issn | 0022-2836 1089-8638 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Computer Simulation domain structure electron microscopy Microscopy, Electron neutron scattering Neutrons Ribonuclease H Ribonucleoproteins - chemistry Ribonucleoproteins - ultrastructure Ribosomes - chemistry RNP particles Scattering, Radiation Thermus thermophilus Thermus thermophilus - chemistry Ultracentrifugation |
| title | Structure of a Beheaded 30 S Ribosomal Subunit from Thermus thermophilus |
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