Eintrag weiter verarbeiten
Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme
Gespeichert in:
| Zeitschriftentitel: | RNA |
|---|---|
| Personen und Körperschaften: | , , |
| In: | RNA, 12, 2006, 3, S. 387-395 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
|
| Schlagwörter: |
| author_facet |
GUO, FENG GOODING, ANNE R. CECH, THOMAS R. GUO, FENG GOODING, ANNE R. CECH, THOMAS R. |
|---|---|
| author |
GUO, FENG GOODING, ANNE R. CECH, THOMAS R. |
| spellingShingle |
GUO, FENG GOODING, ANNE R. CECH, THOMAS R. RNA Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme Molecular Biology |
| author_sort |
guo, feng |
| spelling |
GUO, FENG GOODING, ANNE R. CECH, THOMAS R. 1355-8382 1469-9001 Cold Spring Harbor Laboratory Molecular Biology http://dx.doi.org/10.1261/rna.2198206 <jats:p>Although general mechanisms of RNA folding and catalysis have been elucidated, little is known about how ribozymes achieve structural stability at high temperature. A previous in vitro evolution experiment identified a small number of mutations that significantly increase the thermostability of the tertiary structure of the <jats:italic>Tetrahymena</jats:italic> ribozyme. Because we also determined the crystal structure of this thermostable ribozyme, we have for the first time the opportunity to compare the structural interactions and thermodynamic contributions of individual nucleotides in a ribozyme. We investigated the contribution of five mutations to thermostability by using temperature gradient gel electrophoresis. Unlike the case with several well-studied proteins, the effects of individual mutations on thermostability of this RNA were highly context dependent. The three most important mutations for thermostability were actually destabilizing in the wild-type background. A269G and A304G contributed to stability only when present as a pair, consistent with their proximity in the ribozyme structure. In an evolutionary context, this work supports and extends the idea that one advantage of protein enzyme systems over an RNA world is the ability of proteins to accumulate stabilizing single-site mutations, whereas RNA may often require much rarer double mutations to improve the stability of both its tertiary and secondary structures.</jats:p> Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the <i>Tetrahymena</i> ribozyme RNA |
| doi_str_mv |
10.1261/rna.2198206 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI2MS9ybmEuMjE5ODIwNg |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI2MS9ybmEuMjE5ODIwNg |
| institution |
DE-Zi4 DE-Gla1 DE-15 DE-Pl11 DE-Rs1 DE-14 DE-105 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 |
| imprint |
Cold Spring Harbor Laboratory, 2006 |
| imprint_str_mv |
Cold Spring Harbor Laboratory, 2006 |
| issn |
1355-8382 1469-9001 |
| issn_str_mv |
1355-8382 1469-9001 |
| language |
English |
| mega_collection |
Cold Spring Harbor Laboratory (CrossRef) |
| match_str |
guo2006comparisonofcrystalstructureinteractionsandthermodynamicsforstabilizingmutationsinthetetrahymenaribozyme |
| publishDateSort |
2006 |
| publisher |
Cold Spring Harbor Laboratory |
| recordtype |
ai |
| record_format |
ai |
| series |
RNA |
| source_id |
49 |
| title |
Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_unstemmed |
Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_full |
Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_fullStr |
Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_full_unstemmed |
Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_short |
Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_sort |
comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the <i>tetrahymena</i> ribozyme |
| topic |
Molecular Biology |
| url |
http://dx.doi.org/10.1261/rna.2198206 |
| publishDate |
2006 |
| physical |
387-395 |
| description |
<jats:p>Although general mechanisms of RNA folding and catalysis have been elucidated, little is known about how ribozymes achieve structural stability at high temperature. A previous in vitro evolution experiment identified a small number of mutations that significantly increase the thermostability of the tertiary structure of the <jats:italic>Tetrahymena</jats:italic> ribozyme. Because we also determined the crystal structure of this thermostable ribozyme, we have for the first time the opportunity to compare the structural interactions and thermodynamic contributions of individual nucleotides in a ribozyme. We investigated the contribution of five mutations to thermostability by using temperature gradient gel electrophoresis. Unlike the case with several well-studied proteins, the effects of individual mutations on thermostability of this RNA were highly context dependent. The three most important mutations for thermostability were actually destabilizing in the wild-type background. A269G and A304G contributed to stability only when present as a pair, consistent with their proximity in the ribozyme structure. In an evolutionary context, this work supports and extends the idea that one advantage of protein enzyme systems over an RNA world is the ability of proteins to accumulate stabilizing single-site mutations, whereas RNA may often require much rarer double mutations to improve the stability of both its tertiary and secondary structures.</jats:p> |
| container_issue |
3 |
| container_start_page |
387 |
| container_title |
RNA |
| container_volume |
12 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792334508984369156 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T14:29:33.736Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Comparison+of+crystal+structure+interactions+and+thermodynamics+for+stabilizing+mutations+in+the+Tetrahymena+ribozyme&rft.date=2006-03-01&genre=article&issn=1469-9001&volume=12&issue=3&spage=387&epage=395&pages=387-395&jtitle=RNA&atitle=Comparison+of+crystal+structure+interactions+and+thermodynamics+for+stabilizing+mutations+in+the+%3Ci%3ETetrahymena%3C%2Fi%3E+ribozyme&aulast=CECH&aufirst=THOMAS+R.&rft_id=info%3Adoi%2F10.1261%2Frna.2198206&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792334508984369156 |
| author | GUO, FENG, GOODING, ANNE R., CECH, THOMAS R. |
| author_facet | GUO, FENG, GOODING, ANNE R., CECH, THOMAS R., GUO, FENG, GOODING, ANNE R., CECH, THOMAS R. |
| author_sort | guo, feng |
| container_issue | 3 |
| container_start_page | 387 |
| container_title | RNA |
| container_volume | 12 |
| description | <jats:p>Although general mechanisms of RNA folding and catalysis have been elucidated, little is known about how ribozymes achieve structural stability at high temperature. A previous in vitro evolution experiment identified a small number of mutations that significantly increase the thermostability of the tertiary structure of the <jats:italic>Tetrahymena</jats:italic> ribozyme. Because we also determined the crystal structure of this thermostable ribozyme, we have for the first time the opportunity to compare the structural interactions and thermodynamic contributions of individual nucleotides in a ribozyme. We investigated the contribution of five mutations to thermostability by using temperature gradient gel electrophoresis. Unlike the case with several well-studied proteins, the effects of individual mutations on thermostability of this RNA were highly context dependent. The three most important mutations for thermostability were actually destabilizing in the wild-type background. A269G and A304G contributed to stability only when present as a pair, consistent with their proximity in the ribozyme structure. In an evolutionary context, this work supports and extends the idea that one advantage of protein enzyme systems over an RNA world is the ability of proteins to accumulate stabilizing single-site mutations, whereas RNA may often require much rarer double mutations to improve the stability of both its tertiary and secondary structures.</jats:p> |
| doi_str_mv | 10.1261/rna.2198206 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI2MS9ybmEuMjE5ODIwNg |
| imprint | Cold Spring Harbor Laboratory, 2006 |
| imprint_str_mv | Cold Spring Harbor Laboratory, 2006 |
| institution | DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
| issn | 1355-8382, 1469-9001 |
| issn_str_mv | 1355-8382, 1469-9001 |
| language | English |
| last_indexed | 2024-03-01T14:29:33.736Z |
| match_str | guo2006comparisonofcrystalstructureinteractionsandthermodynamicsforstabilizingmutationsinthetetrahymenaribozyme |
| mega_collection | Cold Spring Harbor Laboratory (CrossRef) |
| physical | 387-395 |
| publishDate | 2006 |
| publishDateSort | 2006 |
| publisher | Cold Spring Harbor Laboratory |
| record_format | ai |
| recordtype | ai |
| series | RNA |
| source_id | 49 |
| spelling | GUO, FENG GOODING, ANNE R. CECH, THOMAS R. 1355-8382 1469-9001 Cold Spring Harbor Laboratory Molecular Biology http://dx.doi.org/10.1261/rna.2198206 <jats:p>Although general mechanisms of RNA folding and catalysis have been elucidated, little is known about how ribozymes achieve structural stability at high temperature. A previous in vitro evolution experiment identified a small number of mutations that significantly increase the thermostability of the tertiary structure of the <jats:italic>Tetrahymena</jats:italic> ribozyme. Because we also determined the crystal structure of this thermostable ribozyme, we have for the first time the opportunity to compare the structural interactions and thermodynamic contributions of individual nucleotides in a ribozyme. We investigated the contribution of five mutations to thermostability by using temperature gradient gel electrophoresis. Unlike the case with several well-studied proteins, the effects of individual mutations on thermostability of this RNA were highly context dependent. The three most important mutations for thermostability were actually destabilizing in the wild-type background. A269G and A304G contributed to stability only when present as a pair, consistent with their proximity in the ribozyme structure. In an evolutionary context, this work supports and extends the idea that one advantage of protein enzyme systems over an RNA world is the ability of proteins to accumulate stabilizing single-site mutations, whereas RNA may often require much rarer double mutations to improve the stability of both its tertiary and secondary structures.</jats:p> Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the <i>Tetrahymena</i> ribozyme RNA |
| spellingShingle | GUO, FENG, GOODING, ANNE R., CECH, THOMAS R., RNA, Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme, Molecular Biology |
| title | Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_full | Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_fullStr | Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_full_unstemmed | Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_short | Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| title_sort | comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the <i>tetrahymena</i> ribozyme |
| title_unstemmed | Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme |
| topic | Molecular Biology |
| url | http://dx.doi.org/10.1261/rna.2198206 |