Polypeptide sequence of the chlorophyll a/b/c-binding protein of the prasinophycean alga Mantoniella squamata

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-b...

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Bibliographic Details
Published inPhotosynthesis research Vol. 40; no. 3; p. 269
Main Authors Schmitt, A, Frank, G, James, P, Staudenmann, W, Zuber, H, Wilhelm, C
Format Journal Article
LanguageEnglish
Published Netherlands 01.06.1994
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Summary: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.
ISSN:0166-8595
DOI:10.1007/bf00034776