Abstract
Luminous organisms use different protein-mediated strategies to modulate light emission color. Here, we report the transient-state kinetic studies of the interaction between photoprotein clytin from Clytia gregaria and its antenna protein, cgreGFP. We propose that cgreGFP forms a transient complex with Ca2+-bound clytin before the excited singlet state of the coelenteramide product is formed. From the spectral distribution and donor-acceptor separation distance, we infer that clytin reaction intermediates may interact only with the middle side part of cgreGFP.
| Original language | English |
|---|---|
| Pages (from-to) | 307-316 |
| Journal | FEBS Letters |
| Volume | 590 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2016 |
Keywords
- aequorin
- bioluminescence
- coelenterazine
- FRET
- obelin
- protein-protein interaction
Fingerprint
Dive into the research topics of 'Transient-state kinetic analysis of complex formation between photoprotein clytin and GFP from jellyfish Clytia gregaria'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver