The localisation of 2‐carboxy‐<scp>d</scp>‐arabinitol 1‐phosphate and inhibition of Rubisco in leaves of <i>Phaseolus vulgaris</i> L

Parry, M. A. J.; Andralojc, P. J.; Lowe, H.; Keys, A. J.

doi:10.1016/s0014-5793(99)00038-1

Cited by 14 publications

(7 citation statements)

References 19 publications

(36 reference statements)

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“…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].…”

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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

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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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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

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“…Indeed, although CA1P is located exclusively in the chloroplast (30,31), and even though kinetic and chloroplast feeding experiments of Glick and Beck (14) provide strong evidence that the synthesis of HBP takes place in the chloroplast, it is not known whether every step in the synthesis of CA1P takes place in the chloroplast. For example, CA is not restricted to the chloroplast and its intracellular distribution is light-dependent (19).…”

Section: Discussionmentioning

confidence: 99%

Elucidating the biosynthesis of 2-carboxyarabinitol 1-phosphate through reduced expression of chloroplastic fructose 1,6-bisphosphate phosphatase and radiotracer studies with ¹⁴ CO ₂

Andralojc

Keys

Koßmann

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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2-Carboxyarabinitol 1-phosphate limits photosynthetic CO2 assimilation at low light because it is a potent, naturally occurring inhibitor of ribulose 1,5-bisphosphate carboxylase͞oxygenase. Evidence is presented that this inhibitor is derived from chloroplastic fructose 1,6-bisphosphate. First, transgenic plants containing decreased amounts of chloroplastic fructose 1,6-bisphosphate phosphatase contained increased amounts of fructose 1,6-bisphosphate and 2-carboxyarabinitol 1-phosphate and greatly increased amounts of the putative intermediates hamamelose and 2-carboxyarabinitol, which in some cases were as abundant as sucrose. Second, French bean leaves in the light were shown to incorporate 14 C from 14 CO2 sequentially into fructose 1,6-bisphosphate, hamamelose bisphosphate, hamamelose monophosphate, hamamelose, and 2-carboxyarabinitol. As shown previously, 14 C assimilated by photosynthesis was also incorporated into 2-carboxyarabinitol 1-phosphate during subsequent darkness.

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“…Other factors contributing to dehydration-related decline of Rubisco activity include (1) the lack of the substrate for the reaction of carboxylation (ATP deficiency decreases the amount of RBP), (2) decreased activity and amount of ATPase (which acts as a coupling factor), (3) loss of RBP recognition sites in the LS of Rubisco (which bind 2-carboxyarabinitol and are thereby inactivated), (4) structural alterations of chloroplasts and Rubisco, and (5) release of Rubisco from damaged plastids, followed by hydrolysis of the enzyme protein [11,14,65,[75][76][77].…”

Section: Dark Reactions Of Photosynthesismentioning

confidence: 99%

Effect of water stress on the photosynthetic apparatus of plants and the protective role of cytokinins: A review

Chernyad’ev

2005

Appl Biochem Microbiol

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In recent years, the definition of the term stress (meaning "strain" in English) has been extended, so that it is now used in reference to higher and lower plants and even microorganisms, as opposed to the original usage implying humans and animals [1][2][3]. The Canadian physiologist Hans Selye, who coined the term in the 1930s [4], believed that the ability of an organism to adaptation is related to concentration and exertion, in the sense of strenuous efforts undertaken to mobilize this organism's defense systems. Similarity of stress reactions in bacteria (the most ancient inhabitants of Earth) [3] to those occurring in contemporary representatives of eukaryotes [1, 2, 4] is currently a welldocumented fact.The most frequent stress effect experienced by plants and their photosynthetic apparatus is water deficiency. The greenhouse effect (which becomes more and more pronounced), increased evaporation and reduction of water basins, elevation of mean annual temperature, and augmented contamination of the atmosphere by anthropogenic microadulterants (first of all, methane and oxides of carbon and nitrogen) [5, 6] may disrupt gas exchange, dark and light reactions of photosynthesis [7][8][9], and the unified hydrodynamic system of water supply, transport, and transpiration, which ensures normal water homeostasis in plants [10].Photosynthesis is particularly sensitive to effects of water deficiency and increased temperature. Even a small decrease in the water potential of a plant causes its stomata to close, which entails ëé 2 deficiency in photosynthesizing tissues and decreases the intensity of photosynthetic assimilation of CO 2 (which is the integral parameter of the process). As the degree of hydration of the tissues decreases, the photosynthetic apparatus of plants undergoes functional changes, which further develop into disruption of its structure [7-9, 11].Studies of the resistance of agricultural plants to water deficiency are of great importance for the understanding of the mechanism of disrupting effects of stress. Such studies are also necessary for developing scientifically well-grounded methods for restoring the operation of the photosynthetic apparatus and increasing its stability (which in turn increase the harvest. However, alterations of the photosynthetic apparatus (and structural and functional characteristics of chloroplasts in particular), taking place under the conditions of water deficiency, are not as well studied as those occurring under the effect of other stress types (e.g., decreased or increased temperatures, deficiency or excess of nitrogen or other nutritive minerals, and amount and quality of light).Plant resistance to water deficiency is related to metabolic changes and functional and structural rearrangements of photosynthesizing tissues. These changes are coordinated by regulatory systems, of which the most important for processes of plant adaptation are those involving cytokinins and other phytohormones. Cytokinins, which regulate multiple functions in plant cells, were shown to ...

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The localisation of 2‐carboxy‐d‐arabinitol 1‐phosphate and inhibition of Rubisco in leaves of Phaseolus vulgaris L

Cited by 14 publications

References 19 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

Elucidating the biosynthesis of 2-carboxyarabinitol 1-phosphate through reduced expression of chloroplastic fructose 1,6-bisphosphate phosphatase and radiotracer studies with ¹⁴ CO ₂

Effect of water stress on the photosynthetic apparatus of plants and the protective role of cytokinins: A review

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The localisation of 2‐carboxy‐d‐arabinitol 1‐phosphate and inhibition of Rubisco in leaves of Phaseolus vulgaris L

Cited by 14 publications

References 19 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

Elucidating the biosynthesis of 2-carboxyarabinitol 1-phosphate through reduced expression of chloroplastic fructose 1,6-bisphosphate phosphatase and radiotracer studies with 14 CO 2

Effect of water stress on the photosynthetic apparatus of plants and the protective role of cytokinins: A review

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Elucidating the biosynthesis of 2-carboxyarabinitol 1-phosphate through reduced expression of chloroplastic fructose 1,6-bisphosphate phosphatase and radiotracer studies with ¹⁴ CO ₂