Structural plasticity of T4 transcription co-activator gp33 revealed by a protease-resistant unfolded state
Copyright © 2017 Elsevier Inc. All rights reserved..
Gene 33 protein (gp33) is a transcriptional coactivator for late genes of the T4 bacteriophage. gp33 possesses a 5-helix bundle core, with unstructured N- and C-terminal regions that account for >50% of the protein sequence. It plays a unique role of interacting with host RNA polymerase, couples transcription with DNA replication, and plays the dual function as repressor and co-activator in phage transcription. Here, we identify protein structural plasticity as the molecular basis of the dual nature in gp33. We find that gp33 has the peculiar property of remaining protease insensitive in its urea-unfolded state. Using NMR studies with spectroscopic measurements, we propose that intra-protein interactions are replaced by protein-urea interactions in gp33. This process not only unfolds gp33 but also renders it protease-resistant. Our studies shed new light on the unique structural malleability of gp33 that might be important in its transition from a repressor to a late transcription co-activator.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2017 |
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| Erschienen: |
2017 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:492 |
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| Enthalten in: |
Biochemical and biophysical research communications - 492(2017), 1 vom: 07. Okt., Seite 61-66 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Mahalakshmi, Radhakrishnan [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 25.09.2017 Date Revised 29.11.2017 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.bbrc.2017.08.038 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a Copyright © 2017 Elsevier Inc. All rights reserved. | ||
| 520 | |a Gene 33 protein (gp33) is a transcriptional coactivator for late genes of the T4 bacteriophage. gp33 possesses a 5-helix bundle core, with unstructured N- and C-terminal regions that account for >50% of the protein sequence. It plays a unique role of interacting with host RNA polymerase, couples transcription with DNA replication, and plays the dual function as repressor and co-activator in phage transcription. Here, we identify protein structural plasticity as the molecular basis of the dual nature in gp33. We find that gp33 has the peculiar property of remaining protease insensitive in its urea-unfolded state. Using NMR studies with spectroscopic measurements, we propose that intra-protein interactions are replaced by protein-urea interactions in gp33. This process not only unfolds gp33 but also renders it protease-resistant. Our studies shed new light on the unique structural malleability of gp33 that might be important in its transition from a repressor to a late transcription co-activator | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Protease resistance | |
| 650 | 4 | |a Protein-urea interaction | |
| 650 | 4 | |a Structural plasticity | |
| 650 | 4 | |a gp33 | |
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| 650 | 7 | |a gene 33 protein, Enterobacteria phage T4 |2 NLM | |
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| 700 | 1 | |a Maurya, Svetlana Rajkumar |e verfasserin |4 aut | |
| 700 | 1 | |a Burdak, Bhawna |e verfasserin |4 aut | |
| 700 | 1 | |a Surti, Parini |e verfasserin |4 aut | |
| 700 | 1 | |a Patel, Manoj S |e verfasserin |4 aut | |
| 700 | 1 | |a Jain, Vikas |e verfasserin |4 aut | |
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