Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: Lessons from a subunit‐crosslinked form of CRP
Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinc...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Saha, Abinit [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
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| Übergeordnetes Werk: |
Enthalten in: FEBS letters - Amsterdam [u.a.] : Elsevier, 1968, 589(2015), 3, Seite 358-363 |
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| Übergeordnetes Werk: |
volume:589 ; year:2015 ; number:3 ; pages:358-363 |
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| DOI / URN: |
10.1016/j.febslet.2014.12.021 |
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| 520 | |a Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S–S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRP cl ), in which the subunits are crosslinked. We demonstrate that CRP cl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically‐determined structure of cAMP–CRP are discussed. The two subunits of CRP were crosslinked by an S–S bond in the presence of cAMP. The crosslinked protein could activate transcription even without cAMP. Unlike CRP, crosslinked CRP did not revert to an inactive conformation at high cAMP. | ||
| 540 | |a Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies | ||
| 540 | |a Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | ||
| 650 | 4 | |a Transcription activation | |
| 650 | 4 | |a Crosslinked CRP | |
| 650 | 4 | |a Activation by cAMP | |
| 650 | 4 | |a Receptors, Cyclic AMP - ultrastructure | |
| 650 | 4 | |a Receptors, Cyclic AMP - genetics | |
| 650 | 4 | |a Transcriptional Activation - genetics | |
| 650 | 4 | |a Receptors, Cyclic AMP - chemistry | |
| 650 | 4 | |a Escherichia coli Proteins - chemistry | |
| 650 | 4 | |a Cyclic AMP - chemistry | |
| 650 | 4 | |a Escherichia coli Proteins - ultrastructure | |
| 650 | 4 | |a DNA-Binding Proteins - ultrastructure | |
| 650 | 4 | |a Escherichia coli Proteins - genetics | |
| 650 | 4 | |a Cyclic AMP - genetics | |
| 650 | 4 | |a Protein Subunits - metabolism | |
| 650 | 4 | |a DNA-Binding Proteins - chemistry | |
| 650 | 4 | |a DNA-Binding Proteins - genetics | |
| 650 | 4 | |a Protein Subunits - chemistry | |
| 700 | 1 | |a Mukhopadhyay, Jayanta |4 oth | |
| 700 | 1 | |a Datta, Ajit Bikram |4 oth | |
| 700 | 1 | |a Parrack, Pradeep |4 oth | |
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10.1016/j.febslet.2014.12.021 doi PQ20160617 (DE-627)OLC1965544436 (DE-599)GBVOLC1965544436 (PRQ)p2016-9746f1908071b7d4dbbfc4f4b3ba9e57cfd3c9270ebfbc76b57b656c86f1a1340 (KEY)0045922420150000589000300358revisitingthemechanismofactivationofcyclicamprecep DE-627 ger DE-627 rakwb eng 570 530 610 DNB Saha, Abinit verfasserin aut Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: Lessons from a subunit‐crosslinked form of CRP 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S–S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRP cl ), in which the subunits are crosslinked. We demonstrate that CRP cl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically‐determined structure of cAMP–CRP are discussed. The two subunits of CRP were crosslinked by an S–S bond in the presence of cAMP. The crosslinked protein could activate transcription even without cAMP. Unlike CRP, crosslinked CRP did not revert to an inactive conformation at high cAMP. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Transcription activation Crosslinked CRP Activation by cAMP Receptors, Cyclic AMP - ultrastructure Receptors, Cyclic AMP - genetics Transcriptional Activation - genetics Receptors, Cyclic AMP - chemistry Escherichia coli Proteins - chemistry Cyclic AMP - chemistry Escherichia coli Proteins - ultrastructure DNA-Binding Proteins - ultrastructure Escherichia coli Proteins - genetics Cyclic AMP - genetics Protein Subunits - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics Protein Subunits - chemistry Mukhopadhyay, Jayanta oth Datta, Ajit Bikram oth Parrack, Pradeep oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 3, Seite 358-363 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:3 pages:358-363 http://dx.doi.org/10.1016/j.febslet.2014.12.021 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2014.12.021/abstract http://www.ncbi.nlm.nih.gov/pubmed/25541491 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 3 358-363 |
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10.1016/j.febslet.2014.12.021 doi PQ20160617 (DE-627)OLC1965544436 (DE-599)GBVOLC1965544436 (PRQ)p2016-9746f1908071b7d4dbbfc4f4b3ba9e57cfd3c9270ebfbc76b57b656c86f1a1340 (KEY)0045922420150000589000300358revisitingthemechanismofactivationofcyclicamprecep DE-627 ger DE-627 rakwb eng 570 530 610 DNB Saha, Abinit verfasserin aut Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: Lessons from a subunit‐crosslinked form of CRP 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S–S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRP cl ), in which the subunits are crosslinked. We demonstrate that CRP cl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically‐determined structure of cAMP–CRP are discussed. The two subunits of CRP were crosslinked by an S–S bond in the presence of cAMP. The crosslinked protein could activate transcription even without cAMP. Unlike CRP, crosslinked CRP did not revert to an inactive conformation at high cAMP. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Transcription activation Crosslinked CRP Activation by cAMP Receptors, Cyclic AMP - ultrastructure Receptors, Cyclic AMP - genetics Transcriptional Activation - genetics Receptors, Cyclic AMP - chemistry Escherichia coli Proteins - chemistry Cyclic AMP - chemistry Escherichia coli Proteins - ultrastructure DNA-Binding Proteins - ultrastructure Escherichia coli Proteins - genetics Cyclic AMP - genetics Protein Subunits - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics Protein Subunits - chemistry Mukhopadhyay, Jayanta oth Datta, Ajit Bikram oth Parrack, Pradeep oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 3, Seite 358-363 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:3 pages:358-363 http://dx.doi.org/10.1016/j.febslet.2014.12.021 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2014.12.021/abstract http://www.ncbi.nlm.nih.gov/pubmed/25541491 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 3 358-363 |
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10.1016/j.febslet.2014.12.021 doi PQ20160617 (DE-627)OLC1965544436 (DE-599)GBVOLC1965544436 (PRQ)p2016-9746f1908071b7d4dbbfc4f4b3ba9e57cfd3c9270ebfbc76b57b656c86f1a1340 (KEY)0045922420150000589000300358revisitingthemechanismofactivationofcyclicamprecep DE-627 ger DE-627 rakwb eng 570 530 610 DNB Saha, Abinit verfasserin aut Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: Lessons from a subunit‐crosslinked form of CRP 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S–S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRP cl ), in which the subunits are crosslinked. We demonstrate that CRP cl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically‐determined structure of cAMP–CRP are discussed. The two subunits of CRP were crosslinked by an S–S bond in the presence of cAMP. The crosslinked protein could activate transcription even without cAMP. Unlike CRP, crosslinked CRP did not revert to an inactive conformation at high cAMP. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Transcription activation Crosslinked CRP Activation by cAMP Receptors, Cyclic AMP - ultrastructure Receptors, Cyclic AMP - genetics Transcriptional Activation - genetics Receptors, Cyclic AMP - chemistry Escherichia coli Proteins - chemistry Cyclic AMP - chemistry Escherichia coli Proteins - ultrastructure DNA-Binding Proteins - ultrastructure Escherichia coli Proteins - genetics Cyclic AMP - genetics Protein Subunits - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics Protein Subunits - chemistry Mukhopadhyay, Jayanta oth Datta, Ajit Bikram oth Parrack, Pradeep oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 3, Seite 358-363 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:3 pages:358-363 http://dx.doi.org/10.1016/j.febslet.2014.12.021 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2014.12.021/abstract http://www.ncbi.nlm.nih.gov/pubmed/25541491 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 3 358-363 |
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10.1016/j.febslet.2014.12.021 doi PQ20160617 (DE-627)OLC1965544436 (DE-599)GBVOLC1965544436 (PRQ)p2016-9746f1908071b7d4dbbfc4f4b3ba9e57cfd3c9270ebfbc76b57b656c86f1a1340 (KEY)0045922420150000589000300358revisitingthemechanismofactivationofcyclicamprecep DE-627 ger DE-627 rakwb eng 570 530 610 DNB Saha, Abinit verfasserin aut Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: Lessons from a subunit‐crosslinked form of CRP 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S–S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRP cl ), in which the subunits are crosslinked. We demonstrate that CRP cl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically‐determined structure of cAMP–CRP are discussed. The two subunits of CRP were crosslinked by an S–S bond in the presence of cAMP. The crosslinked protein could activate transcription even without cAMP. Unlike CRP, crosslinked CRP did not revert to an inactive conformation at high cAMP. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Transcription activation Crosslinked CRP Activation by cAMP Receptors, Cyclic AMP - ultrastructure Receptors, Cyclic AMP - genetics Transcriptional Activation - genetics Receptors, Cyclic AMP - chemistry Escherichia coli Proteins - chemistry Cyclic AMP - chemistry Escherichia coli Proteins - ultrastructure DNA-Binding Proteins - ultrastructure Escherichia coli Proteins - genetics Cyclic AMP - genetics Protein Subunits - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics Protein Subunits - chemistry Mukhopadhyay, Jayanta oth Datta, Ajit Bikram oth Parrack, Pradeep oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 3, Seite 358-363 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:3 pages:358-363 http://dx.doi.org/10.1016/j.febslet.2014.12.021 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2014.12.021/abstract http://www.ncbi.nlm.nih.gov/pubmed/25541491 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 3 358-363 |
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10.1016/j.febslet.2014.12.021 doi PQ20160617 (DE-627)OLC1965544436 (DE-599)GBVOLC1965544436 (PRQ)p2016-9746f1908071b7d4dbbfc4f4b3ba9e57cfd3c9270ebfbc76b57b656c86f1a1340 (KEY)0045922420150000589000300358revisitingthemechanismofactivationofcyclicamprecep DE-627 ger DE-627 rakwb eng 570 530 610 DNB Saha, Abinit verfasserin aut Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: Lessons from a subunit‐crosslinked form of CRP 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S–S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRP cl ), in which the subunits are crosslinked. We demonstrate that CRP cl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically‐determined structure of cAMP–CRP are discussed. The two subunits of CRP were crosslinked by an S–S bond in the presence of cAMP. The crosslinked protein could activate transcription even without cAMP. Unlike CRP, crosslinked CRP did not revert to an inactive conformation at high cAMP. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Transcription activation Crosslinked CRP Activation by cAMP Receptors, Cyclic AMP - ultrastructure Receptors, Cyclic AMP - genetics Transcriptional Activation - genetics Receptors, Cyclic AMP - chemistry Escherichia coli Proteins - chemistry Cyclic AMP - chemistry Escherichia coli Proteins - ultrastructure DNA-Binding Proteins - ultrastructure Escherichia coli Proteins - genetics Cyclic AMP - genetics Protein Subunits - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics Protein Subunits - chemistry Mukhopadhyay, Jayanta oth Datta, Ajit Bikram oth Parrack, Pradeep oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 3, Seite 358-363 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:3 pages:358-363 http://dx.doi.org/10.1016/j.febslet.2014.12.021 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2014.12.021/abstract http://www.ncbi.nlm.nih.gov/pubmed/25541491 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 3 358-363 |
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revisiting the mechanism of activation of cyclic amp receptor protein (crp) by camp in escherichia coli: lessons from a subunit‐crosslinked form of crp |
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Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: Lessons from a subunit‐crosslinked form of CRP |
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Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S–S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRP cl ), in which the subunits are crosslinked. We demonstrate that CRP cl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically‐determined structure of cAMP–CRP are discussed. The two subunits of CRP were crosslinked by an S–S bond in the presence of cAMP. The crosslinked protein could activate transcription even without cAMP. Unlike CRP, crosslinked CRP did not revert to an inactive conformation at high cAMP. |
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Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S–S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRP cl ), in which the subunits are crosslinked. We demonstrate that CRP cl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically‐determined structure of cAMP–CRP are discussed. The two subunits of CRP were crosslinked by an S–S bond in the presence of cAMP. The crosslinked protein could activate transcription even without cAMP. Unlike CRP, crosslinked CRP did not revert to an inactive conformation at high cAMP. |
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Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP–CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally ‘inactive’ to an ‘active’ molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S–S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRP cl ), in which the subunits are crosslinked. We demonstrate that CRP cl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically‐determined structure of cAMP–CRP are discussed. The two subunits of CRP were crosslinked by an S–S bond in the presence of cAMP. The crosslinked protein could activate transcription even without cAMP. Unlike CRP, crosslinked CRP did not revert to an inactive conformation at high cAMP. |
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Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: Lessons from a subunit‐crosslinked form of CRP |
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