ArticleJournal of molecular biology2013
Protein:protein interactions in control of a transcriptional switch.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Rheostatic contributions to protein stability can obscure a position's functional role.Protein science : a publication of the Protein Society · 2024Article
- Emergence of allostery through reorganization of protein residue network architecture.The Journal of chemical physics · 2023Article
- Tuning Allostery through Integration of Disorder to Order with a Residue Network.Biochemistry · 2020Article
- Native mass spectrometry identifies an alternative DNA-binding pathway for BirA from Staphylococcus aureus.Scientific reports · 2019Article
- A conserved regulatory mechanism in bifunctional biotin protein ligases.Protein science : a publication of the Protein Society · 2017Article
- Influence of Secondary-Structure Folding on the Mutually Exclusive Folding Process of GL5/I27 Protein: Evidence from Molecular Dynamics Simulations.International journal of molecular sciences · 2016Article
- Mechanisms of biotin-regulated gene expression in microbes.Synthetic and systems biotechnology · 2016Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Protein partner exchange plays a key role in regulating many biological switches. Although widespread, the mechanisms dictating protein partner identity and, therefore, the outcome of a switch have been determined for a limited number of systems. The Escherichia coli protein BirA undergoes a switch between posttranslational biotin attachment and transcription repression in response to cellular biotin demand. Moreover, the functional switch reflects formation of alternative mutually exclusive protein:protein interactions by BirA. Previous studies provided a set of alanine-substituted BirA variants with altered kinetic and equilibrium parameters of forming these interactions. In this work, DNase I footprinting measurements were employed to investigate the consequences of these altered properties for the outcome of the BirA functional switch. The results support a mechanism in which BirA availability for DNA binding and, therefore, transcription repression is controlled by the rate of the competing protein:protein interaction. However, occupancy of the transcriptional regulatory site on DNA by BirA is exquisitely tuned by the equilibrium constant governing its homodimerization.
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Registered trials
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