Fraction I Protein

Kawashima, and N; Wildman, S. G.

doi:10.1146/annurev.pp.21.060170.001545

Cited by 307 publications

(130 citation statements)

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“…The large subunit has a molecular weight of about 55 000 [3,4], is encoded within chloroplast DNA [5], and is synthesized on chloroplast ribosomes [6]. In contrast, the small subunit has a molecular weight of between 12000 and 16000 [3,4], is the product of a nuclear gene [5], and is synthesized as a precursor of molecular weight 20000 [7,8] on cytoplasmic ribosomes [9]. This precursor enters isolated chloroplasts with concomitant processing to the mature size [7].…”

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confidence: 99%

The Biosynthesis of Ribulose Bisphosphate Carboxylase

Barraclough

Ellis

1979

European Journal of Biochemistry

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Isolated leaf cells from soybean (Glycine max) incorporate [35S]methionine into protein at a linear rate for at least 5 h. Analysis of the products of incorporation by one-dimensional and two-dimensional polyacrylamide gel electrophoresis shows that major products are the large and small subunits of the chloroplast enzyme, ribulose bisphosphate carboxylase. The large subunit is synthesized by chloroplast ribosomes and the small subunit by cytoplasmic ribosomes. Addition of chloramphenicol to the cells reduces incorporation into the large subunit without affecting incorporation into the products of cytoplasmic ribosomes. Addition of cycloheximide or 2-(4-methyl-2,6-dinitroanilino)-N-methylpropionamide stops incorporation into the small subunit, but large subunit continues to be made for at least 4 h. For accurate estimates of incorporation into the large subunit, it is essential to use two-dimensional gel electrophoresis, because the large subunit region on one-dimensional gels is contaminated with the products of cytoplasmic ribosomes. Newly synthesized large subunits continue to enter complete molecules of ribulose bisphosphate carboxylase in the absence of small subunit synthesis. These results suggest that, in contrast to the situation in algal cells, the synthesis of the two subunits of ribulose bisphosphate carboxylase in the different subcellular compartments of higher plant cells is not tightly coupled over short time periods, and that a pool of small subunits exists in these cells. The results are discussed in relation to possible mechanisms for the integration of the synthesis of the large and small subunits of ribulose bisphosphate carboxylase.

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confidence: 99%

The Biosynthesis of Ribulose Bisphosphate Carboxylase

Barraclough

Ellis

1979

European Journal of Biochemistry

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“…We suspected that this preparation of PCH contained RuDPCase. The latter constitutes up to 50% of the total protein present in etiolated bean leaf extracts (1,13), and has a similar size to the holochrome. We subjected purified spinach RuDPCase to electrophoretic analysis and found that peaks Bi, Cl, Plant Physiol.…”

Section: Resultsmentioning

confidence: 99%

Analysis of the Subunit Structure of Protochlorophyllide Holochrome by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

Canaani

Sauer²

1977

Plant Physiol.

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The subunit structue of protochlorophyllide holochrome (PCH) and chlorophyllide holochrome (CH) In this paper we examine the subunit structure of PCH purified from dark-grown bean leaves. The fate of the pigmentprotein complex after photoreduction and after the completion of the dark spectroscopic shift (22) MATERIALS AND METHODS PREPARATION OF HOLOCHROMEBean seedlings (Phaseolus vulgaris var. red kidney) were grown on vermiculite 12 + 2 days in the dark at 22 C. The leaves (50-lOOg) were harvested and ground in a buffer containing 10 mM tris-HCl (pH 8.5), 2 mM MgSO4, 1 mm EDTA, and 25% (v/ v) glycerol. In some cases, Triton X-100 (in final concentration of 0.06%, v/v) was added to the extracting solution and is referred to as buffer + Triton. All manipulations were done in a cold room (4 C) under a green safelight. Two different methods were used for preparation of PCH.Method 1. The leaves were ground in buffer + Triton in a Waring Blendor during four 60-sec intervals, separated by 5 min. The homogenate was filtered through six layers of cheesecloth and centrifuged at 78,000g in a Beckman (model L-2) ultracentrifuge (No. 30 rotor) at 0 C for 1 hr. The supernatant was treated with a 50% PEG-6,000 solution to a final concentration of 17% and centrifuged at 48,000g (-2 C) in a Sorvall RC-2B centrifuge for 1 hr.

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“…This most abundant plant protein masqueraded for many years as 'Fraction one' protein (Wildman and Bonner 1947;Kawashima and Wildman 1970) before its carboxylation activity was uncovered, beginning in 1954 (for historical accounts, see Weissbach and Horecker 1989; A.A. Benson, this issue; and S. Wildman, this issue). Many years later, its bifunctionality was revealed by discovery of its oxygenase activity (Bowes et al 1971).…”

Section: Pre-activase History -A Complex and Schizophrenic Rubiscomentioning

confidence: 99%

The discovery of Rubisco activase — yet another story of serendipity

Portis¹,

Salvucci²

2005

Discoveries in Photosynthesis

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A brief history of Rubisco (ribulose bisphosphate carboxylase oxygenase) research and the events leading to the discovery and initial characterization of Rubisco activase are described. Key to the discovery was the chance isolation of a novel Arabidopsis photosynthesis mutant. The characteristics of the mutant suggested that activation of Rubisco was not a spontaneous process in vivo, but involved a heritable factor. The search for the putative factor by 2D electrophoresis identified two polypeptides, genetically linked to Rubisco activation, that were missing in chloroplasts from the mutant. An assay for the activity of these polypeptides, which were given the name Rubisco activase, was developed after realizing the importance of including ribulose bisphosphate (RuBP) in the assay. The requirement for ATP and the subsequent identification of activase as an ATPase came about fortuitously, the result of a RuBP preparation that was contaminated with adenine nucleotides. Finally, the ability of activase to relieve inhibition of the endogenous Rubisco inhibitor, 2-carboxyarabinitol 1-phosphate, provided an early indication of the mechanism by which activase regulates Rubisco.Abbreviations: CA1P -2-carboxyarabinitol 1-phosphate; FBP -fructose bisphosphate; RuBP -ribulose bisphosphate; Rubisco -ribulose bisphosphate carboxylase oxygenase; Ru5P -ribulose 5-phosphate; SBP -sedoheptulose bisphosphate 'Much discussion, both inside and outside the lecture halls, centered upon the potentially important reports of endogenous compounds which inhibit or activate RuBPCO. The debate was fiercest over reports by M. Salvucci, A. Portis and co-workers of the presence in some tissues of a protein which is involved in the activation of RuBPCO. The suggestion that the protein is an enzyme, hence the name RuBPCO activase, appeared to raise some hackles.' J. A. M. Holtum and E. Latzko, 1987 Pre-activase history -a complex and schizophrenic RubiscoA brief look at some of the history of Rubisco research reveals a saga of surprises that will set an appropriate stage for describing the discovery of Rubisco activase. This most abundant plant protein masqueraded for many years as 'Fraction one' protein (Wildman and Bonner 1947;Kawashima and Wildman 1970) before its carboxylation activity was uncovered, beginning in 1954 (for historical accounts, see Weissbach and Horecker 1989; A.A. Benson, this issue; and S. Wildman, this issue). Many years later, its bifunctionality was revealed by discovery of its oxygenase activity (Bowes et al. 1971). The oxygenase

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Fraction I Protein

Cited by 307 publications

References 0 publications

The Biosynthesis of Ribulose Bisphosphate Carboxylase

The Biosynthesis of Ribulose Bisphosphate Carboxylase

Analysis of the Subunit Structure of Protochlorophyllide Holochrome by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

The discovery of Rubisco activase — yet another story of serendipity

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