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. 1979 Nov;64(5):828–832. doi: 10.1104/pp.64.5.828

Characterization of the 32,000 Dalton Chloroplast Membrane Protein

III. Probing Its Biological Function in Spirodela1

Steven A Weinbaum a,2, Jonathan Gressel a, Avi Reisfeld a,3, Marvin Edelman a
PMCID: PMC543372  PMID: 16661063

Abstract

The rapidly turning over, photoinduced thylakoid protein, P-32000, is the main pulse-labeled membrane polypeptide in the chloroplasts of Spirodela oligorrhiza, yet little is known of its physiological function. Two hypotheses are tested: that P-32000 synthesis is necessary for thylakoid biogenesis; that it directly participates in photosynthesis. Spirodela cultures were dissected into expanding and fully mature tissue. Fronds from both developmental stages transcribed a 0.5 × 106 dalton RNA likely to be the message for P-32000. As to the protein itself, synthesis occurred in both types of tissue but was considerably enhanced in the fully mature state. Thus, a purely transient, developmental function for P-32000 during thylakoid biogenesis appears ruled out. Low concentrations of d-threo-chloramphenicol severely suppressed P-32000 synthesis but not its turnover. As a result, fronds depleted in P-32000 were obtained. However, photoassimilation of CO2 remained at 86% of normal in tissue > 80% depleted of P-32000. Thus, P-32000 did not appear to be rate-limiting, suggesting that it does not serve as a direct, integral part of the photosynthetic pathway.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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