ArticleJournal of molecular biology2008
Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Biotin protein ligase as you like it: Either extraordinarily specific or promiscuous protein biotinylation.Proteins · 2024Review
- Protein oligomerization as a metabolic control mechanism: Application to apoE.Protein science : a publication of the Protein Society · 2019Article
- A conserved regulatory mechanism in bifunctional biotin protein ligases.Protein science : a publication of the Protein Society · 2017Article
- Review
- Mechanisms of biotin-regulated gene expression in microbes.Synthetic and systems biotechnology · 2016Review
- Biotin and Lipoic Acid: Synthesis, Attachment, and Regulation.EcoSal Plus · 2014Article
- Fatty acid synthesis in Escherichia coli and its applications towards the production of fatty acid based biofuels.Biotechnology for biofuels · 2014Article
- Modeling protein association mechanisms and kinetics.Current opinion in structural biology · 2013Review
- Protein:protein interactions in control of a transcriptional switch.Journal of molecular biology · 2013Article
- A large solvent isotope effect on protein association thermodynamics.Biochemistry · 2013Article
- Mapping the Deltex-binding surface on the notch ankyrin domain using analytical ultracentrifugation.Journal of molecular biology · 2011Article
- The use of analytical sedimentation velocity to extract thermodynamic linkage.Biophysical chemistry · 2011Article
- In vivo tests of thermodynamic models of transcription repressor function.Biophysical chemistry · 2011Article
- Biotinylation, a post-translational modification controlled by the rate of protein-protein association.The Journal of biological chemistry · 2011Article
- Biochemical properties and biological function of a monofunctional microbial biotin protein ligase.Biochemistry · 2010Article
- The switch regulating transcription of the Escherichia coli biotin operon does not require extensive protein-protein interactions.Chemistry & biology · 2010Article
- Kinetics of association and dissociation of HIV-1 reverse transcriptase subunits.Biochemistry · 2009Article
- Thermodynamic and structural investigation of bispecificity in protein-protein interactions.Journal of molecular biology · 2009Article
- Biotin sensing at the molecular level.The Journal of nutrition · 2009Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Proteins can perform completely distinct functions in response to the particular partners that they bind to. Consequently, determination of the mechanism of functional regulation in such systems requires elucidation of the mechanism switching between binding partners. The central protein of the Escherichia coli biotin regulatory system, BirA, switches between its function as a metabolic enzyme or a transcriptional repressor in response to binding either the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase or a second BirA monomer. These two protein-protein interactions are structurally mutually exclusive. The results of earlier studies suggest that the system is regulated by kinetic partitioning between the two protein-protein interactions. In this work, sedimentation velocity was employed to monitor the partitioning directly. The results indicate similar equilibrium parameters governing formation of the two protein-protein interactions. Kinetic analysis of the sedimentation velocity data indicated that holoBirA dimerization is governed by very slow forward and reverse rate constants. The slow kinetics of holoBirA dimerization combined with fluctuations in the intracellular apoBCCP pool are critical determinants in partitioning BirA between its distinct biological functions.
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Registered trials
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