The Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease RelE
Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, RelE. The molecular basis for recognition of the ribosome and mRNA by RelE and the mechanism of cleavage are unkn...
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| Veröffentlicht in: | Cell 2009-12, Vol.139 (6), p.1084-1095 |
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| creator | Neubauer, Cajetan Gao, Yong-Gui Andersen, Kasper R. Dunham, Christine M. Kelley, Ann C. Hentschel, Jendrik Gerdes, Kenn Ramakrishnan, V. Brodersen, Ditlev E. |
| description | Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, RelE. The molecular basis for recognition of the ribosome and mRNA by RelE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli RelE in isolation (2.5 Å) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 Å) and after (3.6 Å) cleavage. RelE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2′-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in RelE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. These structures provide detailed insight into the translational regulation on the bacterial ribosome by mRNA cleavage. |
| doi_str_mv | 10.1016/j.cell.2009.11.015 |
| format | Article |
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During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, RelE. The molecular basis for recognition of the ribosome and mRNA by RelE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli RelE in isolation (2.5 Å) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 Å) and after (3.6 Å) cleavage. RelE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2′-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in RelE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. These structures provide detailed insight into the translational regulation on the bacterial ribosome by mRNA cleavage.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/j.cell.2009.11.015</identifier><identifier>PMID: 20005802</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Bacterial Toxins - chemistry ; Bacterial Toxins - metabolism ; Catalysis ; Codons ; Conserved sequence ; Crystal structure ; Endonuclease ; Escherichia coli ; Escherichia coli - chemistry ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Gene expression ; Hydrolysis ; Models, Molecular ; Nucleotides ; PROTEINS ; Ribosomes ; Ribosomes - chemistry ; Ribosomes - metabolism ; RNA, Messenger - metabolism ; RNA, Ribosomal, 16S - metabolism ; rRNA 16S ; Stacking ; Stringent response ; Thermus thermophilus ; Thermus thermophilus - metabolism ; Translation</subject><ispartof>Cell, 2009-12, Vol.139 (6), p.1084-1095</ispartof><rights>2009 Elsevier Inc.</rights><rights>2009 ELL & Excerpta Medica. 2009 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4665-e698d3297f4de8053040209ebc48975e574ddbc0d20c60be27c42d1e148dbb6e3</citedby><cites>FETCH-LOGICAL-c4665-e698d3297f4de8053040209ebc48975e574ddbc0d20c60be27c42d1e148dbb6e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0092867409014275$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20005802$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Neubauer, Cajetan</creatorcontrib><creatorcontrib>Gao, Yong-Gui</creatorcontrib><creatorcontrib>Andersen, Kasper R.</creatorcontrib><creatorcontrib>Dunham, Christine M.</creatorcontrib><creatorcontrib>Kelley, Ann C.</creatorcontrib><creatorcontrib>Hentschel, Jendrik</creatorcontrib><creatorcontrib>Gerdes, Kenn</creatorcontrib><creatorcontrib>Ramakrishnan, V.</creatorcontrib><creatorcontrib>Brodersen, Ditlev E.</creatorcontrib><title>The Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease RelE</title><title>Cell</title><addtitle>Cell</addtitle><description>Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, RelE. The molecular basis for recognition of the ribosome and mRNA by RelE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli RelE in isolation (2.5 Å) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 Å) and after (3.6 Å) cleavage. RelE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2′-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in RelE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. 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During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, RelE. The molecular basis for recognition of the ribosome and mRNA by RelE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli RelE in isolation (2.5 Å) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 Å) and after (3.6 Å) cleavage. RelE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2′-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in RelE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. 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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; EZB-FREE-00999 freely available EZB journals |
| subjects | Bacterial Toxins - chemistry Bacterial Toxins - metabolism Catalysis Codons Conserved sequence Crystal structure Endonuclease Escherichia coli Escherichia coli - chemistry Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Gene expression Hydrolysis Models, Molecular Nucleotides PROTEINS Ribosomes Ribosomes - chemistry Ribosomes - metabolism RNA, Messenger - metabolism RNA, Ribosomal, 16S - metabolism rRNA 16S Stacking Stringent response Thermus thermophilus Thermus thermophilus - metabolism Translation |
| title | The Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease RelE |
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