Evidence for function of the ferredoxin/thioredoxin system in the reductive activation of target enzymes of isolated intact chloroplasts

Crawford, Nancy A.; Droux, Michel; Kosower, Nechama S.; Buchanan, Bob B.

doi:10.1016/0003-9861(89)90273-7

Cited by 106 publications

(57 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The expression of the mRNA coding for DdTRXl-3 are coregulated during development, and maximal mRNA levels are seen in the phase of the life cycle, when growth is arrested (Wetterauer et al, 1992). Many of the described in vivo functions of TRX are linked to biosynthesis and growth, such as ribonucleotide reduction in E. coli (Reichard, 1988), sulfur assimilation in E. coli and Saccharomyces cerevisiae (Russel et al, 1990;Muller, 1991), methionine-sulfoxide reduction (Russel et al, 1990), regulation of plant metabolism (Crawford et al, 1989), growth of plant protoplasts (Marty and Meyer, 1991) and stimulation of lymphocytes (Wollman et al, 1989, Tagaya et al, 1989. Since the expression pattern of Dictyosteliurn TRX does not fit this notion, we wanted to compare the enzymic capacity of the Dictyostelium TRX to those of described TRX from other species.…”

Section: Discussionmentioning

confidence: 99%

Biochemical characterization of thioredoxin 1 from Dictyostelium discoideum

Wetterauer

Veron

Miginiac‐Maslow

et al. 1992

European Journal of Biochemistry

View full text Add to dashboard Cite

Multiple genes for thioredoxins (TRX) have been demonstrated in Dictyostelium discoideum. We expressed the cDNA for one of these genes (DdTrxl) in E. coli and purified the protein to homogeneity. The interaction with classic substrates as well as TRX reductases was analysed. It reacted with every tested substrate : insulin, NADP-dependent malate dehydrogenase and fructose-1,6-bisphosphatase. With a So.5 of 20 pM, the reactivity with the fructose-l,6-bisphosphatase is the highest ever found for a heterologous TRX. DdTRXl itself is accepted as a substrate by the chloroplast ferredoxindependent TRX reductase, as well as by the E. coli NADPH-dependent TRX reductase. Thus, the Dictyostelium TRX is functionally promiscuous. Its reactivity with insulin, chloroplast NADPdependent malate dehydrogenase and ferredoxin-dependent TRX reductase resemble those of other TRX. It is, however, clearly different in its good interaction with chloroplast fructose-l,6-bisphosphatase and in its poor interaction with E. cnli NADP-dependent TRX reductase.

show abstract

Section: Discussionmentioning

confidence: 99%

Biochemical characterization of thioredoxin 1 from Dictyostelium discoideum

Wetterauer

Veron

Miginiac‐Maslow

et al. 1992

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…In chloroplasts, thioredoxin is coupled to the photosynthetic electron transport via ferredoxin and ferredoxin: thioredoxin reductase. This reaction pathway is highly active and modulates various chloroplast enzymes by redox control of the sulfhydryl groups (Crawford et at., 1989;Scheibe, 1996). It is tempting to speculate that BAS1 is also activated by this pathway.…”

Section: The Exact Enzymatic Regeneration Of Oxidized Bas1mentioning

confidence: 99%

The plant 2‐Cys peroxiredoxin BAS1 is a nuclear‐encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants

Baier

Dietz²

1997

The Plant Journal

216

140

View full text Add to dashboard Cite

“…Leegood et al, 1982;Rebeille and Hatch, 1986a, 198613;Sassenrath et al, 1990). Although a kinetic explanation has generally been given for this difference in behavior, citing slower reoxidation of CF (Shahak, 1985;Selman-Reimer and Selman, 1988) than of the carbon reduction cycle enzymes (Crawford et al, 1989), evidence is beginning to emerge that the redox midpoint potentials of the thiol groups of thioredoxin-modulated enzymes may play a central role in determining the regulatory behavior. Equilibrium redox titrations reveal that, although the regulatory sulfhydryl on CF is nearly equipotential with thioredoxin f at -270 mV (Ort and Oxborough, 1992;Hutchison, 1993), the chloroplast bisphosphatases are about 40 mV more reducing Hatch, 1986a, 1986b;Hutchison, 1993).…”

Section: Dlscusslonmentioning

confidence: 99%

Mutants of Chloroplast Coupling Factor Reduction in Arabidopsis

et al. 1994

View full text Add to dashboard Cite

We have devised a two-step screening strategy for the selection of chloroplast coupling factor reduction mutants from an Mz population of Arabidopsis fhaliana. The selection strategy relies on a lowered energetic threshold for catalytic activation of the enzyme that has been shown to accompany thioredoxin-mediated reduction of a cysteine bridge on the y subunit of coupling factor. W e selected first for plants that grew poorly under low irradiance but performed satisfactorily at high irradiance when the transmembrane electrochemical potential of hydrogen ions is large and competent to maintain a high leve1 of coupling factor activation without y subunit reduction. In the second step of the screen we monitored the flashinduced electrochromic change to select putative coupling factor reduction mutants from other sorts of mutations that shared the phenotype of poor growth and vigor when transferred from high to low irradiance. Among the mutants selected, one appears incapable of reducing coupling factor, whereas another behaves as though coupling factor is at least partially reduced even in darkadapted plants.The light-dependent regulation of key enzymes in photosynthesis is a central factor in ensuring efficient energy storage in the highly dynamic diurna1 light environment of natural habitats. The thylakoid membrane CF is one of the enzymes of the chloroplast regulated by light, presumably to ensure efficient ATP synthesis under favorable energetic conditions and to prevent the wasteful hydrolysis of stromal ATP in the dark. Experimental evidence points to a regulatory hierarchy for CF involving three principal components: ApH+, the oxidation state of the CF y subunit Cys bridge, and the interactive binding of ATP, ADP, and Pi to the CF (eg.

show abstract

Evidence for function of the ferredoxin/thioredoxin system in the reductive activation of target enzymes of isolated intact chloroplasts

Cited by 106 publications

References 35 publications

Biochemical characterization of thioredoxin 1 from Dictyostelium discoideum

Biochemical characterization of thioredoxin 1 from Dictyostelium discoideum

The plant 2‐Cys peroxiredoxin BAS1 is a nuclear‐encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants

Mutants of Chloroplast Coupling Factor Reduction in Arabidopsis

Contact Info

Product

Resources

About