Premium
Connecting color with assembly in the fluorescent B‐phycoerythrin protein complex
Author(s) -
Leney Aneika C.,
Tschanz Aline,
Heck Albert J. R.
Publication year - 2018
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14331
Subject(s) - phycoerythrin , fluorescence , chemistry , pigment , biology , biochemistry , biophysics , flow cytometry , microbiology and biotechnology , physics , organic chemistry , quantum mechanics
Phycoerythrin is the major light‐harvesting pigment protein in red algae and is nowadays widely used as a fluorescent probe in biotechnological applications such as flow cytometry and immunofluorescence microscopy. In addition, it has had substantial economic impact due to its potential as a natural food colorant. However, knowledge on the precise molecular composition of phycoerythrin is limited. Here, we use a combination of high‐resolution native mass spectrometry ( MS ) and fluorescence spectroscopy to characterize the assembly properties of the B‐phycoerythrin protein complex from Porphyridium cruentum . Our data highlight the stabilizing role of the γ subunit in the intact B‐phycoerythrin protein complex. In addition, by native MS we monitor B‐phycoerythrin (dis)assembly intermediates, providing insight into which species contribute to B‐phycoerythrins color and the factors that give B‐phycoerythrin its highly fluorescent properties. Together, the data provide significant insights into the structural properties of B‐phycoerythrin which is beneficial for its use within the biotechnology industry.