Identification of the elusive pyruvate reductase of Chlamydomonas reinhardtii chloroplasts

Burgess, Steven J., Hussein, Taha, Yeoman, Justin A., Iamshanova, Oksana, Chan, Kher Xing, Boehm, Marko, Behrends, Volker ORCID:, Bundy, Jacob G., Bialek, Wojciech and Murray, James W. (2015) Identification of the elusive pyruvate reductase of Chlamydomonas reinhardtii chloroplasts. Plant Cell Physiology, 57 (1). ISSN 0032-0781

Full text not available from this repository.


Under anoxic conditions the green alga Chlamydomonas
reinhardtii activates various fermentation pathways leading
to the creation of formate, acetate, ethanol and small
amounts of other metabolites including D-lactate and hydrogen.
Progress has been made in identifying the enzymes
involved in these pathways and their subcellular locations;
however, the identity of the enzyme involved in reducing
pyruvate to D-lactate has remained unclear. Based on sequence
comparisons, enzyme activity measurements, X-ray
crystallography, biochemical fractionation and analysis
of knock-down mutants, we conclude that pyruvate
reduction in the chloroplast is catalyzed by a tetrameric
NAD+-dependent D-lactate dehydrogenase encoded by
Cre07.g324550. Its expression during aerobic growth supports
a possible function as a ‘lactate valve’ for the export
of lactate to the mitochondrion for oxidation by cytochrome-
dependent D-lactate dehydrogenases and by glycolate
dehydrogenase. We also present a revised spatial model
of fermentation based on our immunochemical detection of
the likely pyruvate decarboxylase, PDC3, in the cytoplasm.

Item Type: Article
Identifier: 10.1093/pcp/pcv167
Keywords: Biohydrogen; Chlamydomonas; Fermentation; LDH; Lactate.
Subjects: Natural sciences > Cell and molecular biology
Depositing User: Eilish McLaughlin
Date Deposited: 13 Jun 2024 14:15
Last Modified: 13 Jun 2024 14:15

Actions (login required)

View Item View Item