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Books > Science & Mathematics > Biology, life sciences > Microbiology (non-medical)
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Algal Development - Molecular and Cellular Aspects (Paperback, Softcover reprint of the original 1st ed. 1987)
Loot Price: R2,770
Discovery Miles 27 700
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Algal Development - Molecular and Cellular Aspects (Paperback, Softcover reprint of the original 1st ed. 1987)
Series: Proceedings in Life Sciences
Expected to ship within 10 - 15 working days
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Donate to Against Period Poverty
Total price: R2,780
Discovery Miles: 27 800
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Although the 32 kOa-polypeptide (0-1) is a minor component of
thyla- koids in algae and higher plants. much attention has been
focused on it. It was shown to be the binding site for herbicides
(Pfister et al. 1981). the rapidly synthesized polypeptide of
thylakoid membranes (Edelman and Reisfeld 1978; Owens et al. 1982)
and to participate in Qa binding (Arntzen et al. 1984; Kyle et al.
1984; Ohad et al. 1984). Measurements of the stoichiometry of the
various PS II polypeptides in C. reinhardii showed that thylakoids
contain about one herbicide binding polypeptide per one PS II unit
and the accelerated light sti- mulated turnover of the 32
kOa-polypeptide was postulated to be the consequence of its
function in quinone reduction. Based on comparison of amino acid
sequence and hydropathy profile homologies of 0-1 and 0-2 with the
subunits of the bacterial photosystem. recently a model was
presented. in which the reaction center of photosystem II in algae
and higher plants is formed by the polypeptides 0-1 and 0-2 (Trebst
1986). The structural gene of the 32 kOa-polypeptide (psbA) has
been mapped on the chloroplast DNA and cloned from various plant
species (for a review: Kyle 1985). The polypeptide is synthesized
as a precursor on ribosomes bound to unstacked lamellae and there
proc- essed to its mature form (Edelman and Reisfeld 1978; Herrin
and Michaels 1985). In C. reinhardii the 0-1 polypeptide is
phosphorylat- ed by a light-activated membrane bound kinase.
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