Immobility of phycobilins in the thylakoid lumen of a cryptophyte suggests that protein diffusion in the lumen is very restricted
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
Grant support
C17403/2
Biotechnology and Biological Sciences Research Council - United Kingdom
Wellcome Trust - United Kingdom
PubMed
19166839
DOI
10.1016/j.febslet.2009.01.016
PII: S0014-5793(09)00025-8
Knihovny.cz E-resources
- MeSH
- Models, Biological MeSH
- Time Factors MeSH
- Cryptophyta metabolism MeSH
- Diffusion MeSH
- Fluorescence Recovery After Photobleaching MeSH
- Phycobilins metabolism MeSH
- Proteins metabolism MeSH
- Thylakoids metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Phycobilins MeSH
- Proteins MeSH
The thylakoid lumen is an important photosynthetic compartment which is the site of key steps in photosynthetic electron transport. The fluidity of the lumen could be a major constraint on photosynthetic electron transport rates. We used Fluorescence Recovery After Photobleaching in cells of the cryptophyte alga Rhodomonas salina to probe the diffusion of phycoerythrin in the lumen and chlorophyll complexes in the thylakoid membrane. In neither case was there any detectable diffusion over a timescale of several minutes. This indicates very restricted phycoerythrin mobility. This may be a general feature of protein diffusion in the thylakoid lumen.
References provided by Crossref.org
Lipid polymorphism of plant thylakoid membranes. The dynamic exchange model - facts and hypotheses
Fast Diffusion of the Unassembled PetC1-GFP Protein in the Cyanobacterial Thylakoid Membrane
Presence of state transitions in the cryptophyte alga Guillardia theta
Phycobilisome Mobility and Its Role in the Regulation of Light Harvesting in Red Algae
Mobility of photosynthetic proteins
