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STRUCTURAL RELATIONSHIPS OF THE PHOTOSYSTEM I AND PHOTOSYSTEM II CHLOROPHYLL a/b AND a/c LIGHT‐HARVESTING APOPROTEINS OF PLANTS AND ALGAE
Author(s) -
Plumley F. Gerald,
Martinson Tracey A.,
Herrin David L.,
Ikeuchi Masahiko,
Schmidt Gregory W.
Publication year - 1993
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1993.tb02270.x
Subject(s) - chlamydomonas reinhardtii , light harvesting complex , photosystem ii , biology , thylakoid , chlamydomonas , biochemistry , photosynthesis , chlorophyll , euglena gracilis , botany , chloroplast , gene , mutant
Polyclonal antibodies against four different apoproteins of either the chlorophyll (Chl) a/b light‐harvesting antenna of photosystem I or II, or a chlorophyll‐protein complex homologous to CP26 from Chlamydomonas reinhardtii , crossreact with11–13 thylakoid proteins of Chlamydomonas, Euglena gracilis and higher plants. The number of antigenically‐related proteins correlates with the quantity of light‐harvesting chlorophyll‐protein complex (LHC) gene types that have been sequenced in higher plants. The antibodies also react specifically with Chi a/c‐ binding proteins of three diatoms and Coccolithophora sp. as determined by immunoblot and Ouchterlony assays. Four to six crossreacting proteins are observed in each chromophyte species and a functional role for some can be deduced by antibody reactivity. It appears that despite major differences in the structures of their pigment ligands, at least some domains of Chl‐binding LHC apoproteins have been conserved during their evolution, possibly functioning in protein: protein, as opposed to pigment: protein, interactions in photosynthetic membranes.