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Effect of Triacontanol on Chlamydomonas
Author(s) -
Robert L. Houtz,
S. K. Ries,
N. E. Tolbert
Publication year - 1985
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.79.2.365
Subject(s) - chlamydomonas reinhardtii , ribulose , chlamydomonas , photosynthesis , spinacia , triacontanol , oxygenase , rubisco , biochemistry , chemistry , biology , botany , enzyme , chloroplast , mutant , gene
Increased photosynthetic CO(2) assimilation by Chlamydomonas reinhardtii cells treated with triacontanol (TRIA) was not due to changes in glycolate excretion, CO(2) compensation point, or the sensitivity of photosynthetic CO(2) assimilation to O(2). Kinetic analysis of TRIA-treated cells showed that the increase in photosynthetic CO(2) assimilation was a result of an increase in the apparent V(max) for intact cells. The total activity of ribulose-P(2) carboxylase/oxygenase was higher in cell lysates from TRIA-treated cells. However quantification of this enzyme concentration by binding of [(14)C]carboxyarabinitol-P(2) did not show an increase in TRIA-treated cells. Thus, there was an increase in the specific activity of ribulose-P(2) carboxylase/oxygenase extracted from Chlamydomonas cells treated with TRIA. TRIA alone had no effect on the activity of the enzyme in cell lysates from Chlamydomonas or purified from spinach (Spinacia oleracea L.) leaves.The ribulose-P(2) pool was 50 to 60% higher in cells treated with TRIA that were assayed for photosynthetic CO(2) assimilation at high- and low-CO(2). TRIA also increased ribulose-P(2) levels in the absence of CO(2) in the light with atmospheres of N(2) or N(2) with 21% O(2).

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