Abstract
The primary structure of the Chla/b/c-binding protein from Mantoniella squamata is determined. This is the first report that protein sequencing reveals one modified amino acid resulting in a LHCP-specific TFA-cleavage site. The comparison of the sequence of Mantoniella with other Chla/b-and Chla/c-binding proteins shows that the modified amino acid is located in a region which is highly conserved in all these proteins. The alignment also reveals that the LHCP of Mantoniella is related to the Chla/b-binding proteins. Finally, possible Chl-binding regions are discussed.
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Abbreviations
- a.m.u.:
-
atomic mass unit
- LHC:
-
light-harvesting complex
- LHC II:
-
major LHC of Photosystem II
- LHCP:
-
light-harvesting chlorophyll-binding protein
- LSIMS:
-
liquid secondary ion mass spectrometry
- TFA:
-
trifluoroacetic acid
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Schmitt, A., Frank, G., James, P. et al. Polypeptide sequence of the chlorophyll a/b/c-binding protein of the prasinophycean alga Mantoniella squamata . Photosynth Res 40, 269–277 (1994). https://doi.org/10.1007/BF00034776
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DOI: https://doi.org/10.1007/BF00034776