C. Passaquet et C. Lichtl, MOLECULAR STUDY OF A LIGHT-HARVESTING APOPROTEIN OF GIRAUDYOPSIS STELLIFER (CHRYSOPHYCEAE), Plant molecular biology, 29(1), 1995, pp. 135-148
We have isolated a gene from a library of nuclear DNA for a chlorophyl
l a/c-binding protein (named Cac for chi a/c by analogy with Cab for c
hi a/b) of a chromophyte alga, Giraudyopsis stellifer, and sequenced i
t. The comparison of the deduced amino acid sequence with other chi a/
c- and chi a/b-binding protein sequences shows that structural and fun
ctional features, i.e. the arrangement 'en X' of the two A and B trans
membrane helices and the putative chi a-binding sites, are shared by b
oth Chlorophyta and Chromophyta. Moreover, in contrast to Chlorophyta,
a very strong identity is found among Chromophyta in the C helix, sug
gesting a major function associated to this specific region. Neverthel
ess, the primary structure of the apoprotein does not seem affected by
the pigment composition in Chromophyta. As in the few other examples
currently known, we confirm that the cac genes are nuclear-encoded and
are part of a multigenic family. Northern blots, performed on poly(A)
(+) mRNA from G. stellifer, give evidence that the cac gene is light-i
nduced at a transcriptional level and that no expression can be observ
ed in the dark.