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Coupling of binding and differential subdomain folding of the intrinsically disordered transcription factor CREB.
- Source :
-
FEBS letters [FEBS Lett] 2023 Apr; Vol. 597 (7), pp. 917-932. Date of Electronic Publication: 2022 Dec 19. - Publication Year :
- 2023
-
Abstract
- The cyclic AMP response element binding protein (CREB) contains a basic leucine zipper motif (bZIP) that forms a coiled coil structure upon dimerization and specific DNA binding. Although this state is well characterized, key features of CREB bZIP binding and folding are not well understood. We used single-molecule Förster resonance energy transfer (smFRET) to probe conformations of CREB bZIP subdomains. We found differential folding of the basic region and leucine zipper in response to different binding partners; a strong and previously unreported DNA-independent dimerization affinity; folding upon binding to nonspecific DNA; and evidence of long-range interdomain interactions in full-length CREB that modulate DNA binding. These studies provide new insights into DNA binding and dimerization and have implications for CREB function.<br /> (© 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 597
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 36480418
- Full Text :
- https://doi.org/10.1002/1873-3468.14554