Kinetic Parameters for tmRNA Binding to Alanyl-tRNA Synthetase and Elongation Factor Tu from Escherichia coli
Aminoacylation and transportation of tmRNA to stalled ribosomes constitute prerequisite steps for trans-translation, a process facilitating the release of stalled ribosomes from 3‘ ends of truncated mRNAs and the degradation of incompletely synthesized proteins. Kinetic analysis of the aminoacylatio...
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| Veröffentlicht in: | Biochemistry (Easton) 2000-03, Vol.39 (10), p.2652-2658 |
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| container_title | Biochemistry (Easton) |
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| creator | Barends, Sharief Wower, Jacek Kraal, Barend |
| description | Aminoacylation and transportation of tmRNA to stalled ribosomes constitute prerequisite steps for trans-translation, a process facilitating the release of stalled ribosomes from 3‘ ends of truncated mRNAs and the degradation of incompletely synthesized proteins. Kinetic analysis of the aminoacylation of tmRNA indicates that tmRNA has both a lower affinity and a lower turnover number than cognate tRNAAla for alanyl-tRNA synthetase, resulting in a 75-fold lower k cat/K M value. The association rate constant of Ala-tmRNA for elongation factor Tu in complex with GTP is about 150-fold lower than that of Ala-tRNAAla, whereas its dissocation rate constant is about 5-fold lower. These observations can be interpreted to suggest that additional factors facilitate tmRNA binding to ribosomes. |
| doi_str_mv | 10.1021/bi992439d |
| format | Article |
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Kinetic analysis of the aminoacylation of tmRNA indicates that tmRNA has both a lower affinity and a lower turnover number than cognate tRNAAla for alanyl-tRNA synthetase, resulting in a 75-fold lower k cat/K M value. The association rate constant of Ala-tmRNA for elongation factor Tu in complex with GTP is about 150-fold lower than that of Ala-tRNAAla, whereas its dissocation rate constant is about 5-fold lower. These observations can be interpreted to suggest that additional factors facilitate tmRNA binding to ribosomes.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>10704215</pmid><doi>10.1021/bi992439d</doi><tpages>7</tpages></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Acylation Alanine-tRNA Ligase - genetics Alanine-tRNA Ligase - metabolism Biopolymers - metabolism Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli - metabolism Kinetics Peptide Elongation Factor Tu - genetics Peptide Elongation Factor Tu - metabolism RNA, Messenger - metabolism RNA, Transfer, Ala - genetics RNA, Transfer, Ala - metabolism Thermodynamics Transcription, Genetic |
| title | Kinetic Parameters for tmRNA Binding to Alanyl-tRNA Synthetase and Elongation Factor Tu from Escherichia coli |
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