Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast and cytosol enzyme from spinach

Pelzer-Reith, Birgit; Penger, Anja; Schnarrenberger, Claus

doi:10.1007/bf00019948

Cited by 45 publications

(29 citation statements)

References 34 publications

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“…By contrast, four FBA p isoforms were identified. In green leaves of maize (Zea mays), wheat (Triticum aestivum), spinach (Spinacia oleracea), and pea (Pisum sativum), most of the FBA activity (approximately 90%) is chloroplastic (Schnarrenberger and Krü ger, 1986;Pelzer-Reith et al, 1993), and a small decrease in FBA p activity in potato (Solanum tuberosum) leaves resulted in the inhibition of photosynthesis and starch synthesis (Haake et al, 1998). However, in germinating castor seed, FBA activity is mostly cytosolic, representing two-thirds of the activity (Moorhead et al, 1994).…”

Section: Five Glycolytic Proteins Showed An Increased Number Of Isofomentioning

confidence: 99%

Quantitative Proteomics of Seed Filling in Castor: Comparison with Soybean and Rapeseed Reveals Differences between Photosynthetic and Nonphotosynthetic Seed Metabolism

2009

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Seed maturation or seed filling is a phase of development that plays a major role in the storage reserve composition of a seed. In many plant seeds photosynthesis plays a major role in this process, although oilseeds, such as castor (Ricinus communis), are capable of accumulating oil without the benefit of photophosphorylation to augment energy demands. To characterize seed filling in castor, a systematic quantitative proteomics study was performed. Two-dimensional gel electrophoresis was used to resolve and quantify Cy-dye-labeled proteins expressed at 2, 3, 4, 5, and 6 weeks after flowering in biological triplicate. Expression profiles for 660 protein spot groups were established, and of these, 522 proteins were confidently identified by liquid chromatography-tandem mass spectrometry by mining against the castor genome. Identified proteins were classified according to function, and the most abundant groups of proteins were involved in protein destination and storage (34%), energy (19%), and metabolism (15%). Carbon assimilatory pathways in castor were compared with previous studies of photosynthetic oilseeds, soybean (Glycine max) and rapeseed (Brassica napus). These comparisons revealed differences in abundance and number of protein isoforms at numerous steps in glycolysis. One such difference was the number of enolase isoforms and their sum abundance; castor had approximately six times as many isoforms as soy and rapeseed. Furthermore, Rubisco was 11-fold less prominent in castor compared to rapeseed. These and other differences suggest some aspects of carbon flow, carbon recapture, as well as ATP and NADPH production in castor differs from photosynthetic oilseeds.Castor (Ricinus communis) is a model heterotrophic oilseed that contains up to 60% fatty acids compared to approximately 20% and 40% in autotrophic oilseeds soybean (Glycine max) and rapeseed (Brassica napus), respectively (Weiss, 2000). Castor oil is a major component of many industrial lubricants and is currently of special interest, as it is being considered for biofuel use (Baldwin and Cossar, 2008;Dyer et al., 2008;Scholz and da Silva, 2008). With its high fatty acid content and recently sequenced genome, castor is a model plant for studying carbon assimilation in nonphotosynthetic oilseeds.

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Section: Five Glycolytic Proteins Showed An Increased Number Of Isofomentioning

confidence: 99%

Quantitative Proteomics of Seed Filling in Castor: Comparison with Soybean and Rapeseed Reveals Differences between Photosynthetic and Nonphotosynthetic Seed Metabolism

2009

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“…CI-FBAs are present mostly in eukaryotes especially in animals (Rutter 1964, Marsh andLebherz 1992) and higher plants (Rutter 1964, Schnarrenberger et al 1990), whereas CII-FBAs occur mainly in prokaryotes (Henze et al 1998) and to a lesser degree, in some eukaryotes such as fungi and yeast (Rutter 1964, Schwelberger et al 1989. CI-and CII-FBAs share no homology between their gene sequences of DNA (Kelly and Tolan 1986, Marsh and Lebherz 1992, Pelzer-Reith et al 1993, therefore it is presumed that the genes for the two FBA classes appeared and evolved independently from each other. Chloroplasts of all photosynthetic eukaryotes, ranging from macroalgae to higher plants possess CI-FBAs, whereas in the cytosol, both classes of FBA are present and functional (Plaumann et al 1997.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Class-I and Class-II Fructose-1,6-bisphosphate Aldolases from the Cyanobacterium Synechocystis sp. PCC 6803

Nakahara

Yamamoto

Miyake

et al. 2003

Plant and Cell Physiology

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;The whole genome sequence database for Synechocystis sp. PCC 6803 has revealed the presence of genes encoding class-I (CI) and class-II (CII) fructose-1,6-bisphosphate aldolases (FBAs) in this organism. Two types of FBA from Synechocystis sp. PCC 6803 were separated by chromatography on phenyl-Sepharose. The activity of the enzyme in the major peak was inhibited by the presence of 25 mM EDTA; however, the activity in the minor peak was not. Therefore, the FBA in the former fractions was designated as CII-FBA, and in the latter designated as CI-FBA. CI-FBA was functionally redundant in Synechocystis sp. PCC 6803, while no disruptant for the gene encoding CII-FBA was obtained under photoautotrophic conditions. The kinetic parameters of CI-and CII-FBAs purified from Synechocystis sp. PCC 6803 in the cleavage reaction of FBP were generally similar, except in their reactivity for SBP. The SBP/FBP activity ratio of the CII-FBA was two times higher than that of the CI-FBA.

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“…In respect to class I and I1 aldolases, a11 cyanobacteria analyzed so far contain only class I1 aldolases and no class I aldolases, as higher plants do (see Ikawa et al, 1972;March and Lebherz, 1992). In addition, class I1 aldolases from yeast (Alefounder et al, 1989) and E. coli (Schwelberger et al, 1989) do not share any sequence homology with class I aldolases of higher plants and animals (Jonathan et al, 1956;March and Lebherz, 1992;Pelzer-Reith et al, 1993). Therefore, a direct evolution of a class I1 aldolase of cyanobacteria or of cyanoplasts of C. paradoxa to the chloroplast class I aldolase of higher plants has to be excluded.…”

Section: Dlscusslonmentioning

confidence: 99%

“…In cyanobacteria so far, class 11 aldolases have been found (Rutter, 1964;Ikawa et al, 1972;March and Lebherz, 1992), whereas class I aldolases are the enzymes in chloroplasts of green algae and higher plants (Rutter, 1964;Bukowiecki and Anderson, 1974;Schnarrenberger et al, 1990). A direct evolution of the cyanobacterial to the chloroplastic enzyme has to be excluded because of the lack of sequence homology between class I and class I1 aldolases (Alefounder et al, 1989;Schwelberger et al, 1989;March and Lebherz, 1992;Pelzer-Reith et al, 1993). Therefore, it was of interest to determine the type of aldolase in the cyanoplasts (for terminology, see of Cyanophora paradoxa.…”

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confidence: 99%

Two Distinct Aldolases of Class II Type in the Cyanoplasts and in the Cytosol of the Alga Cyanophora paradoxa

et al. 1994

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Two aldolases from the alga Cyanophora paradoxa (Glaucocystophyta) can be separated by chromatography on diethylaminoethyl-Fradogel. The two aldolases are inhibited by 1 mM ethylenediaminetetraacetate (EDTA) and, therefore, are class II aldolases. When cells of C. paradoxa were fractionated, one aldolase was associated with the cytosol fraction and the other was associated with the cyanoplast fraction. The Km(fructose-1,6-bisphosphate) was 600 p~ for the cytosolic aldolase and 340 p~ for the cyanoplast aldolase. The activity of the cytosolic aldolase was increased up to 4-fold by 100 mM K+ and slightly inhibited by li+ and Cs+, whereas the cyanoplast aldolase was not affected by these ions. lnactivation by 1 mM EDTA could be partly restored by the addition of Coz+ or Mn2+ and to a lesser extent by Znz+ or Mgz+. The molecular masses of the native cytosolic and cyanoplast aldolases are about 90 and 85 kD, respectively, as estimated by velocity centrifugation in sucrose gradients. lmplications for the evolution of class I and II aldolases in chloroplasts of higher plants and algae will be discussed.

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Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast and cytosol enzyme from spinach

Cited by 45 publications

References 34 publications

Quantitative Proteomics of Seed Filling in Castor: Comparison with Soybean and Rapeseed Reveals Differences between Photosynthetic and Nonphotosynthetic Seed Metabolism

Quantitative Proteomics of Seed Filling in Castor: Comparison with Soybean and Rapeseed Reveals Differences between Photosynthetic and Nonphotosynthetic Seed Metabolism

Purification and Characterization of Class-I and Class-II Fructose-1,6-bisphosphate Aldolases from the Cyanobacterium Synechocystis sp. PCC 6803

Two Distinct Aldolases of Class II Type in the Cyanoplasts and in the Cytosol of the Alga Cyanophora paradoxa

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