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A systems approach to model natural variation in reactive properties of bacterial ribosomes
BACKGROUND: Natural variation in protein output from translation in bacteria and archaea may be an organism-specific property of the ribosome. This paper adopts a systems approach to model the protein output as a measure of specific ribosome reactive properties in a ribosome-mediated translation app...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2488324/ https://www.ncbi.nlm.nih.gov/pubmed/18620602 http://dx.doi.org/10.1186/1752-0509-2-62 |
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author | Jackson, Julius H Schmidt, Thomas M Herring, Patricia A |
author_facet | Jackson, Julius H Schmidt, Thomas M Herring, Patricia A |
author_sort | Jackson, Julius H |
collection | PubMed |
description | BACKGROUND: Natural variation in protein output from translation in bacteria and archaea may be an organism-specific property of the ribosome. This paper adopts a systems approach to model the protein output as a measure of specific ribosome reactive properties in a ribosome-mediated translation apparatus. We use the steady-state assumption to define a transition state complex for the ribosome, coupled with mRNA, tRNA, amino acids and reaction factors, as a subsystem that allows a focus on the completed translational output as a measure of specific properties of the ribosome. RESULTS: In analogy to the steady-state reaction of an enzyme complex, we propose a steady-state translation complex for mRNA from any gene, and derive a maximum specific translation activity, T(a(max)), as a property of the ribosomal reaction complex. T(a(max) )has units of a-protein output per time per a-specific mRNA. A related property of the ribosome, [Formula: see text] , has units of a-protein per time per total RNA with the relationship [Formula: see text] = ρ(a )T(a(max)), where ρ(a )represents the fraction of total RNA committed to translation output of P(a )from gene a message. T(a(max) )as a ribosome property is analogous to k(cat )for a purified enzyme, and [Formula: see text] is analogous to enzyme specific activity in a crude extract. CONCLUSION: Analogy to an enzyme reaction complex led us to a ribosome reaction model for measuring specific translation activity of a bacterial ribosome. We propose to use this model to design experimental tests of our hypothesis that specific translation activity is a ribosomal property that is subject to natural variation and natural selection much like V(max )and K(m )for any specific enzyme. |
format | Text |
id | pubmed-2488324 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-24883242008-07-29 A systems approach to model natural variation in reactive properties of bacterial ribosomes Jackson, Julius H Schmidt, Thomas M Herring, Patricia A BMC Syst Biol Research Article BACKGROUND: Natural variation in protein output from translation in bacteria and archaea may be an organism-specific property of the ribosome. This paper adopts a systems approach to model the protein output as a measure of specific ribosome reactive properties in a ribosome-mediated translation apparatus. We use the steady-state assumption to define a transition state complex for the ribosome, coupled with mRNA, tRNA, amino acids and reaction factors, as a subsystem that allows a focus on the completed translational output as a measure of specific properties of the ribosome. RESULTS: In analogy to the steady-state reaction of an enzyme complex, we propose a steady-state translation complex for mRNA from any gene, and derive a maximum specific translation activity, T(a(max)), as a property of the ribosomal reaction complex. T(a(max) )has units of a-protein output per time per a-specific mRNA. A related property of the ribosome, [Formula: see text] , has units of a-protein per time per total RNA with the relationship [Formula: see text] = ρ(a )T(a(max)), where ρ(a )represents the fraction of total RNA committed to translation output of P(a )from gene a message. T(a(max) )as a ribosome property is analogous to k(cat )for a purified enzyme, and [Formula: see text] is analogous to enzyme specific activity in a crude extract. CONCLUSION: Analogy to an enzyme reaction complex led us to a ribosome reaction model for measuring specific translation activity of a bacterial ribosome. We propose to use this model to design experimental tests of our hypothesis that specific translation activity is a ribosomal property that is subject to natural variation and natural selection much like V(max )and K(m )for any specific enzyme. BioMed Central 2008-07-13 /pmc/articles/PMC2488324/ /pubmed/18620602 http://dx.doi.org/10.1186/1752-0509-2-62 Text en Copyright © 2008 Jackson et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Jackson, Julius H Schmidt, Thomas M Herring, Patricia A A systems approach to model natural variation in reactive properties of bacterial ribosomes |
title | A systems approach to model natural variation in reactive properties of bacterial ribosomes |
title_full | A systems approach to model natural variation in reactive properties of bacterial ribosomes |
title_fullStr | A systems approach to model natural variation in reactive properties of bacterial ribosomes |
title_full_unstemmed | A systems approach to model natural variation in reactive properties of bacterial ribosomes |
title_short | A systems approach to model natural variation in reactive properties of bacterial ribosomes |
title_sort | systems approach to model natural variation in reactive properties of bacterial ribosomes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2488324/ https://www.ncbi.nlm.nih.gov/pubmed/18620602 http://dx.doi.org/10.1186/1752-0509-2-62 |
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