Evidence map›Paper›PMID 18620602›Full record

ArticleBMC systems biology2008

A systems approach to model natural variation in reactive properties of bacterial ribosomes.

Julius H Jackson, Thomas M Schmidt, Patricia A Herring

Abstract read
In one paragraph

Article in BMC systems biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Julius H JacksonDepartment of Microbiology & Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA. jhjacksn@msu.edu
Thomas M Schmidt
Patricia A Herring

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundNatural 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.

resultsIn 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, Ta(max), as a property of the ribosomal reaction complex. Ta(max) has units of a-protein output per time per a-specific mRNA. A related property of the ribosome, T a(max), has units of a-protein per time per total RNA with the relationshipT a(max) = rho(a)Ta(max), where rho(a) represents the fraction of total RNA committed to translation outpout of P(a) from gene a message. Ta(max) as a ribosome property is analogous to k(cat) for a purified enzyme, and Ta(max) is analogous to enzyme specific activity in a crude extract.

conclusionAnalogy 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 Vmax and Km for any specific enzyme.

Indexed as

Protein BiosynthesisAdaptation, BiologicalBacteriaCatalysisKineticsModels, GeneticRibosomal ProteinsRibosomesRNA, BacterialRNA, MessengerRNA, Transfer, Amino Acid-SpecificSpecies SpecificitySystems BiologyRibosomal ProteinsRNA, BacterialRNA, MessengerRNA, Transfer, Amino Acid-Specific

Identifiers

PMID18620602
PMCPMC2488324

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LicenceCC BY
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.