6533b7d1fe1ef96bd125cd59
RESEARCH PRODUCT
Polypeptide sequence of the chlorophyll a/b/c-binding protein of the prasinophycean alga Mantoniella squamata.
Gerhard FrankAnnemarie SchmittHerbert ZuberPeter JamesChristian WilhelmWerner Staudenmannsubject
chemistry.chemical_classificationChlorophyll abiologyBinding proteinProtein primary structureCell BiologyPlant ScienceGeneral Medicinebiology.organism_classificationBiochemistryMolecular biologyAmino acidLight-harvesting complexchemistry.chemical_compoundProtein sequencingBiochemistrychemistryMantoniellaPeptide sequencedescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1994-06-01 | Photosynthesis research |