Altered Rubisco activity and amounts of a daytime tightbinding inhibitor in transgenic tobacco expressing limiting amounts of phosphoribulokinase

Paul, M. J.; Andralojc, P. J.; Banks, F. M.; Parry, M. A. J.; Knight, Jacqueline S.; Gray, John C.; Keys, A. J.

doi:10.1093/jxb/47.12.1963

Cited by 12 publications

(7 citation statements)

References 9 publications

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“…During the day, considerable protection against proteolysis could be provided by Rubisco carbamoylation (which is promoted in the light by an ATP‐dependent process catalysed by Rubisco activase) and/or by substrate turnover (Table 2). In addition, intermediates in the synthesis of CA1P [43] or tight binding inhibitors of Rubisco, distinct from CA1P, present in light‐adapted leaves [14,44–46] may afford similar protection under conditions in which Rubisco activity is not saturated.…”

Section: Discussionmentioning

confidence: 99%

“…We are acquiring new data which show that naturally occurring Rubisco inhibitors, present in illuminated leaves [14,44,45], may protect Rubisco from stress‐induced inactivation ([52] and S. Khan, P. J. Andralojc & M. A. J. Parry, unpublished data). Hence, the protection conferred on Rubisco by CA1P may be one aspect of a more general type of protective strategy in vivo.…”

Section: Discussionmentioning

confidence: 99%

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2′‐Carboxy‐D‐arabitinol 1‐phosphate protects ribulose 1,5‐bisphosphate carboxylase/oxygenase against proteolytic breakdown

Khan

Andralojc

Lea

et al. 1999

European Journal of Biochemistry

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Trypsin-catalysed cleavage of purified ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the resultant irreversible loss of carboxylase activity were prevented by prior incubation with the naturally occurring nocturnal Rubisco inhibitor 2 H -carboxy-d-arabitinol 1-phosphate (CA1P), as well as with ribulose 1,5-bisphosphate (RuBP), Mg 21 and CO 2 . CA1P also protected Rubisco from loss of activity caused by carboxypeptidase A. When similar experiments were carried out using soluble chloroplast proteases, CA1P was again able to protect Rubisco against proteolytic degradation and the consequent irreversible loss of catalytic activity. Thus, CA1P prevents the proteolytic breakdown of Rubisco by endogenous and exogenous proteases. In this way, CA1P may affect the amounts of Rubisco protein available for photosynthetic CO 2 assimilation. Rubisco turnover (in the presence of RuBP, Mg 21 and CO 2 ) may confer similar protection against proteases in the light. Rubisco is only active when an essential lysine residue within the large subunit is carbamoylated with CO 2 followed by co-ordination of Mg 21 by this carbamate to form a ternary complex at the catalytic site. This process is ordered and reversible, and the equilibrium between the two forms of Rubisco (noncarbamoylated, R 0 , and carbamoylated ternary complex, R) depends on the concentrations of CO 2 and Mg 21 . 2-Carboxy-d-arabitinol 1-phosphate (CA1P) is a naturally occurring transition-state analogue of the carboxylase reaction, which has the capacity to bind tightly to the active site of Rubisco and thus inhibit both the carboxylase and oxygenase activities of the enzyme [3,4]. CA1P is found exclusively in chloroplasts [5] and is synthesized during periods of low light or darkness [6,7]. The amount of CA1P present in leaves is dependent on the plant species and the duration of the dark period [8,9]. In Phaseolus vulgaris, there is enough CA1P present to block all the active sites of Rubisco while in species such as potato, soybean and tobacco there is enough CA1P present to block about 50% of the active sites of Rubisco [6,8]. On transition from dark to light, Rubisco activase promotes the release of CA1P from the catalytic site of Rubisco [10], and free CA1P is rendered noninhibitory by the action of a lightactivated CA1P-phosphatase [11±13]. In vitro, CA1P bound to the active site of Rubisco can be released by treatment with sulfate ions and subsequently removed by gel filtration, to restore the activity of the enzyme [14].During leaf senescence, proteins are catabolized to amino acids, which are transported to the appropriate sinks, which are frequently developing fruits [15,16]. As Rubisco is a major store of nitrogen in actively photosynthesizing mature leaves, the regulation of the breakdown of this enzyme has been subject to considerable study [17±19]. High protease activity has been detected in the vacuole [20], a ubiquitin-targeting system described in the cytosol [21] and light-dependent or ATP-dependent proteolytic breakdown described in ...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

2′‐Carboxy‐D‐arabitinol 1‐phosphate protects ribulose 1,5‐bisphosphate carboxylase/oxygenase against proteolytic breakdown

Khan

Andralojc

Lea

et al. 1999

European Journal of Biochemistry

Self Cite

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“…This inhibitor is subsequently degraded by a light-dependent phosphatase (7). In a similar pattern, Rubisco can also accumulate inhibitors during the day through the formation of inhibitory compounds during catalysis that remain bound to the active site and hinder catalysis (8,9). These inhibitors include pentodiulose-P 2 and xylulose-P 2 , and the in vitro formation of these compounds has been well characterized (10 -18).…”

Section: Rubiscomentioning

confidence: 99%

Small Oligomers of Ribulose-bisphosphate Carboxylase/Oxygenase (Rubisco) Activase Are Required for Biological Activity

Keown

Griffin

Mertens

et al. 2013

Journal of Biological Chemistry

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Background: Rubisco activase optimizes photosynthesis in plants, yet the arrangement of subunits is unclear. Results: The oligomeric state and biological function of Rubisco activase are dependent on protein concentration. Conclusion: Rubisco activase does not need to be hexameric for full activity. Significance: Understanding the functioning of Rubisco activase is an important step in determining how it regulates Rubisco.

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“…Transgenic plants with altered amounts of ribulose-1, 5-bisphosphate carboxylase-oxygenase (Rubisco, EC 4.1.1.39) revolutionized the analysis of photosynthesis and its interaction with the whole plant (Stitt and Schulze 1994;Quick et al 1991b). However, the content of Rubisco accounts for 15% to 35% of total leaf N in C 3 species, and a decrease in the amount of Rubisco substantially disrupts the N balance of the plant, making it difficult to establish direct links between photosynthesis and growth and allocation (Woodrow and Berry 1988;Paul et al 1996). The study of phosphoribulokinase (PRK, EC3.1.3.11) has found that only 94% decrease in PRK activity by antisense RNA in transgenic tobacco diminishes photosynthesis at low N level (Banks et al 1999;Habash et al 1996).…”

Section: Introductionmentioning

confidence: 99%

Reduction in SBPase Activity by Antisense RNA in Transgenic Rice Plants: Effect on Photosynthesis, Growth, and Biomass Allocation at Different Nitrogen Levels

Feng

Jiao

et al. 2009

J. Plant Biol.

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Rice cultivar zhonghua11 (Oryza sativa L. ssp. japonica) plants with decreased sedoheptulose-1, 7-bisphosphatase (SBPase) were obtained by transformation with the rice SBPase antisense gene under the control of the maize ubiquitin promoter. The transgenic and wild-type plants were grown at different nitrogen levels (0.1, 1, or 10 mM NH 4 NO 3 ). Growth rates of the seedlings were measured by the changes in dry weight, and the photosynthetic carbon reduction activities and the potential efficiency of photosystem II were measured by CO 2 assimilation and F v /F m , respectively. At low N, there are strong effects on growth and photosynthesis when SBPase was reduced by genetic manipulation. Decreased SBPase activity led to a decrease in the amount of starch accumulated in the leaves at all N levels and the decrease was much more prominent in low N than that in high N, but the starch allocation between shoot and root was unaltered. The analysis of chlorophyll fluorescence and SBPase activity indicated that the decrease of growth and photosynthesis at different N levels were not related to the function of PSII but to the activity of SBPase. Western blot analysis showed the content of SBPase in thylakoid membranes was much more than in the stroma fractions in transgenic plants at low N. Results suggested that low N in addition to a 34% decrease in SBPase activity is sufficient to diminish photosynthesis and limit biomass production. Decreased SBPase activity may reduce the N use efficiency of photosynthesis and growth and alter biomass allocation.

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Altered Rubisco activity and amounts of a daytime tightbinding inhibitor in transgenic tobacco expressing limiting amounts of phosphoribulokinase

Cited by 12 publications

References 9 publications

2′‐Carboxy‐D‐arabitinol 1‐phosphate protects ribulose 1,5‐bisphosphate carboxylase/oxygenase against proteolytic breakdown

2′‐Carboxy‐D‐arabitinol 1‐phosphate protects ribulose 1,5‐bisphosphate carboxylase/oxygenase against proteolytic breakdown

Small Oligomers of Ribulose-bisphosphate Carboxylase/Oxygenase (Rubisco) Activase Are Required for Biological Activity

Reduction in SBPase Activity by Antisense RNA in Transgenic Rice Plants: Effect on Photosynthesis, Growth, and Biomass Allocation at Different Nitrogen Levels

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