Abstract:
:Several lines of evidence support the proposal that the unusual chloroplast-specific lipid acyl group Delta3,trans-hexadecenoic acid (trans-C(16:1)) stimulates the formation or maintenance of the oligomeric form of the light-harvesting chlorophyll a/b complex (LHCP). To assess the functional significance of this apparent association we have analyzed LHCP structure and function in a mutant of Arabidopsis thaliana (L.) which lacks trans-C(16:1) by electrophoretic analysis of the protein-chlorophyll complexes and by measurements of chlorophyll fluorescence under a variety of conditions. By these criteria the putative oligomeric form of LHCP appears to be slightly more labile to detergent-mediated dissociation in the mutant. The oligomeric PSI chlorophyll-protein complex, associated with PSI, was also more labile to detergent-mediated dissociation in the mutant, suggesting a previously unsuspected association of trans-C(16:1) with the PSI complex. However, no significant effect of the mutation on the efficiency of energy transfer from LHCP to the photochemical reaction centers was observed under any of the various conditions imposed. Also, the stability of the chlorophyll-protein complexes to temperature-induced dissociation was unaffected in the mutant. The role of trans-C(16:1) is very subtle or is only conditionally expressed.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
McCourt P,Browse J,Watson J,Arntzen CJ,Somerville CRdoi
10.1104/pp.78.4.853subject
Has Abstractpub_date
1985-08-01 00:00:00pages
853-8issue
4eissn
0032-0889issn
1532-2548journal_volume
78pub_type
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