Light/Dark Modulation of Enzyme Activity in Photosynthesis

Anderson, Louise E.; Ashton, Anthony R.; Mohamed, A. Habib; Scheibe, Renate

doi:10.2307/1308562

Cited by 24 publications

(17 citation statements)

References 22 publications

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“…The kinetic and physical properties of these enzymes, and other mechanisms by which they are reg ulated, will also be reviewed. There have been recent reviews of the biochemis try of C4 photosynthesis (28,31) and the light modulation of other photosyn thetic enzymes, particularly in C3 plants (1)(2)(3)(16)(17)(18), so these areas will not be covered here .…”

Section: C4 Cycle and Its Significance In Photosynthesismentioning

confidence: 99%

Pyruvate,Pi Dikinase and NADP-Malate Dehydrogenase in C4 Photosynthesis: Properties and Mechanism of Light/Dark Regulation

Edwards¹,

Nakamoto²,

Burnell³

et al. 1985

Annu. Rev. Plant. Physiol.

196

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Section: C4 Cycle and Its Significance In Photosynthesismentioning

confidence: 99%

Pyruvate,Pi Dikinase and NADP-Malate Dehydrogenase in C4 Photosynthesis: Properties and Mechanism of Light/Dark Regulation

Edwards¹,

Nakamoto²,

Burnell³

et al. 1985

Annu. Rev. Plant. Physiol.

196

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“…There is much literature on the existence of protein-protein interactions between the components of the ferredoxin-Td activation system, these interactions being responsible of erroneous activating theories earlier described: LEM factors [2], protein modulase [8] and ferralterin [18]. Close associations have also been demonstrated between ferredoxin and ferredoxin-thioredoxin reductase [11], and between Td f and FBPase [24].…”

Section: Introductionmentioning

confidence: 99%

Binding site on pea chloroplast fructose-1,6-bisphosphatase involved in the interaction with thioredoxin

et al. 1996

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When we compare the primary structures of the six chloroplast fructose-1,6-biophosphatases (FBPase) so far sequenced, the existence of a poorly conserved fragment in the region just preceeding the redox regulatory cysteines cluster can be observed. This region is a good candidate for binding of FBPase to its physiological modulator thioredoxin (Td), as this association shows clear differences between species. Using a cDNA clone for pea chloroplast FBPase as template, we have amplified by PCR a DNA insert coding for a 19 amino acid fragment (149Pro-167Gly), which was expressed in pGEMEX-1 as a fusion protein. This protein strongly interacts with pea Td m, as shown by ELISA and Superose 12 gel filtration, depending on pH of the medium. Preliminary assays have shown inhibition of FBPase activity in the presence of specific IgG against the 19 amino acid insert. Surprisingly the fusion protein enhances the FBPase activation in competitive inhibition experiments carried out with FBPase and Td. These results show the fundamental role played by this domain in FBPase-Td binding, not only as docking point for Td, but also by inducing some structural modification in the Td molecule. Taking as model the structural data recently published for spinach photosynthetic FBPase, this sequence from a tertiary and quaternary structural point of view appears available for rearrangement.

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“…The thioredoxin-dependent regulatory cycle of PRK (and of a number of other Calvin-cycle enzymes) in vivo has been deduced from a combination of organellar and in-vitro experiments (reviewed in Anderson 1986;Buchanan 1980). In summary, PRK in illuminated leaves was in an active (Avron and Gibbs 1974;Laing et al 1981 ;Wirtz et al 1982) and reduced form (Crawford et al 1989).…”

Section: Resultsmentioning

confidence: 99%

“…(1) the majority of PRK in darkened leaves, a condition associated with oxidized, inactive enzyme (Anderson 1986;Buchanan 1980), was a constituent of a high-Mr complex (Fig. 2B, D); and (2) fully activated PRK, a condition associated with illuminated, photosynthetically active leaves (Avron and Gibbs 1974;Laing et al 1981 ;Wirtz et al 1982), was not a constituent of any stable multiprotein complex (Fig.…”

Section: Discussionmentioning

confidence: 99%

The aggregation states of spinach phosphoribulokinase

Porter

1990

Planta

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Phosphoribulokinase (PRK; EC 2.1.7.19) is active in illuminated chloroplasts and inactive in darkened chloroplasts. This regulatory mechanism is mediated by thioredoxin-dependent reduction of a kinase disulfide in vivo. Extracts of spinach (Spinacia oleracea L.) leaves in the presence of 10 mM dithiothreitol contain a single 80-kDa form of PRK as judged by gel filtration. Gel filtration of thiol-free extracts of light-harvested tissue shows the presence of two inactive forms of PRK, the 80-kDa form and an aggregate (> 550 kDa) form, but treatment of both forms with dithiothreitol restores kinase activity. Gel filtration following extraction of dark-harvested tissue in the absence of dithiotreitol demonstrates the presence of only the heavier form. Inclusion of 400 mM (NH4)2SO4 in the homogenization buffer during extraction of light-harvested tissue suppresses the formation of the high-M r form of PRK, but does not eliminate the aggregate form observed in extracts of dark-harvested leaves. However, prolonged treatment of extracts from dark-harvested tissue with 400 mM (NH4)2SO4 results in conversion of the high-M r form of phosphoribulokinase to the low-M r form. The data are consistent with the heavier form of phosphoribulokinase being the normal in-vivo aggregation state in the dark, while the lighter form is the normal aggregation state in the light.This research was sponsored jointly by the science and education administration of the U.S. Department of Agriculture under Grant No. 88-37130-3722 from the Competitive Research Grants Office and by the Office of Health and Environmental Research, U.S. Department of Energy under Contract DE-AC05-84OR21400 with Martin Marietta Energy Systems Inc., Oak Ridge, Tenn., USA. The author is Postdoctoral Investigator supported by the U.S. Department of Agriculture through Subcontract No. 88-37130-3722 from the Biology Division of Oak Ridge National Laboratory to the University of Tennessee.

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Light/Dark Modulation of Enzyme Activity in Photosynthesis

Cited by 24 publications

References 22 publications

Pyruvate,Pi Dikinase and NADP-Malate Dehydrogenase in C4 Photosynthesis: Properties and Mechanism of Light/Dark Regulation

Pyruvate,Pi Dikinase and NADP-Malate Dehydrogenase in C4 Photosynthesis: Properties and Mechanism of Light/Dark Regulation

Binding site on pea chloroplast fructose-1,6-bisphosphatase involved in the interaction with thioredoxin

The aggregation states of spinach phosphoribulokinase

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