Ribulose 1,5-bisphosphate carboxylase from the thermophilic, acidophilic alga, Cyanidium caldarium (Geitler)

Ford, T. W.

doi:10.1016/0005-2744(79)90059-7

Cited by 34 publications

(16 citation statements)

References 19 publications

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“…Mol wt determinations reveal 55 kD for the LSU and 15.5 kD for the SSU of RuBPCase. These values are in good agreement with the results of Ford (14). PC and APC were also separated into two subunits with the following mol wt: a-PC, 16.6 kD; #-PC, 20.2 kD; a-APC, 16 kD; and fl-APC, 17.8 kD.…”

Section: Methodssupporting

confidence: 90%

Photo- and Metabolite Regulation of the Synthesis of Ribulose Bisphosphate Carboxylase/Oxygenase and the Phycobiliproteins in the Alga Cyanidium caldarium

Steinmüller¹,

Zetsche²

1984

Plant Physiol.

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Hitherto, the regulation of the synthesis of plastid proteins has mainly been studied in green algae and higher plants. For these plants it is now well established that the synthesis of plastid proteins is under the control of light and phytohormones and in the case of several algae under the control of a metabolizable carbon source in the culture medium (5,8,20,27). The enzyme RuBPCase3 is one ofthe most thoroughly studied plastid proteins in green algae and higher plants.It is composed of eight large and eight small subunits. In green algae and higher plants the LSU is encoded by plastid DNA and synthesized on 70 S ribosomes, while the SSU is encoded in nuclear genes and is synthesized on the 80 S ribosomes of the cytoplasm as a precursor polypeptide (11,13,17,22).In a previous paper (25) we have demonstrated that in the unicellular eukaryotic alga Cyanidium caldarium, the SSU of RuBPCase is synthesized together with the LSU of the enzyme by poly(A)-RNA. Both subunits are synthesized in the size of the mature subunits. These findings suggest that the gene for the SSU of RuBPCase may be encoded in the plastid DNA of this 1 Supported by the Deutsche Forschungsgemeinschaft, Bad Godesberg.

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Section: Methodssupporting

confidence: 90%

Photo- and Metabolite Regulation of the Synthesis of Ribulose Bisphosphate Carboxylase/Oxygenase and the Phycobiliproteins in the Alga Cyanidium caldarium

Steinmüller¹,

Zetsche²

1984

Plant Physiol.

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“…The temperature optimum of T. thyasiris RuBisCO (55 "C) is consistent with the temperature optima reported for other Thiobacillus RuBisCOs (Table 2), but higher than those from the thermophiles Cyanidium caldarium (42 "C) (Ford, 1979) and Chromatium tepidum (50 "C) (Heda & Madigan, 1988). This is not indicative of a thermophilic characteristic since whereas the Cyanidium and Chromatium enzymes were stable at their temperature optima, T. thyasiris RuBisCO was not.…”

Section: Discussionsupporting

confidence: 75%

Kinetic properties of ribulose bisphosphate carboxylase/oxygenase from Thiobacillus thyasiris, the putative symbiont of Thyasira flexuosa (Montagu), a bivalve mussel

Cook

Lanaras

Wood

et al. 1991

Journal of General Microbiology

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Some kinetic properties of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase from Thiobaciffus thyasiris, a marine, facultatively heterotrophic, sulphur-oxidizing bacterium and putative symbiont of Thyasira fixuosa (Montagu), a bivalve mussel, have been determined. The kinetic parameters for the COz/Mg2+-activated enzyme were: K,,,(RuBP) 24.3 pM, K,,,(CO,) 125.5 pM, Km(02) 900 pM and Km(Mg2+) 1.53 mM. The low C o t affinity suggests that T. thyusiris may possess a Cot-concentrating mechanism. RuBP oxygenase activity was inhibited by increasing Cot concentration. Divalent metal ions were essential for RuBP carboxylase activity; activity of the Mg2+-free enzyme could be restored by the addition of Mg2+, Mn2+ or Cat+. The pH optimum was 7.8. The temperature optimum for RuBP carboxylase activity was 55 "C, although the enzyme rapidly lost activity at this temperature. An Arrhenius plot was biphasic, with a break at 40 "C. The activation energies were 55.5 x lo3 J mol-I and 32-9 x lo3 J mol-I over the temperature ranges 10-40 "C and 40-55 "C, respectively. Qlo was 2.12 for any 10 "C increment between 1 0 4 0 "C, and 1.47 between 40-55 "C. RuBP carboxylase activity was stable at 35 "C, the optimum growth temperature of T. fhyasiris and at 7.5 "C, the temperature of the habitat of TiryaSira ~~X U O S U , but the activity was 40% and 3.5%, respectively, of the potential activity at 55 "C. RuBP carboxylase activity was stimulated by NaCl concentrations of up to 0.3 M, with a maximum (33 %), occurring between 0.1 and 0.2 M-Naa. At higher concentrations of NaCl ( > 0.3 M) RuBP carboxylase activity was inhibited.

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“…We have shown here that C. tepidum RuBisCO is also heat stable, at least to 60°C. C. tepidum RuBisCO is therefore the most thermostable of any such enzyme from anoxygenic phototrophs, and is similar in this respect to RuBisCO from the acidophilic, thermophilic alga, Cyanidiiim caldarium [28]. The only RuBisCO reported to be more thermal stable is that from the extremely thermophilic sulfur lithotroph, Thermothrix thiopara [18].…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of the thermostable ribulose‐1,5‐bisphosphate carboxylase/oxygenase from the thermophilic purple bacterium Chromatium tepidum

Heda

Madigan

1989

European Journal of Biochemistry

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The Calvin cycle enzyme ribulose-bisphosphate carboxylase/oxygenase has been purified and characterized from the thermophilic and obligately anaerobic purple sulfur bacterium, Chromatium tepidum. The enzyme is an L8S8 carboxylase with a molecular mass near 550 kDa. N o evidence for a second form of the enzyme lacking small subunits was obtained. C. tepidum ribulose-bisphosphate carboxylase/oxygenase was stable to heating to temperatures of 60°C and could be readily purified in an active form at room temperature. Both carboxylase and oxygenase activities of this enzyme were Mg2 +-dependent and carboxylase activity was sensitive to the effector 6-phosphogluconic acid. The K , for ribulose bisphosphate for the carboxylase activity of the C. tepidurn enzyme was substantially higher than that observed in mesophilic Calvin cycle autotrophs. Amino acid composition and immunological analyses of C. tepidum and Chromatium vinosum ribulose-bisphosphate carboxylases showed the enzymes to be highly related despite significant differences in heat stability. It is hypothesized that thermal stability of C. tepidum ribulose-bisphosphate carboxylase/oxygenase is due to differences in primary structure affecting folding patterns in both the large and small subunits and is clearly not the result of any unique quaternary structure of the thermostable enzyme.Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) catalyzes the first step of C 0 2 fixation in organisms that employ the reductive pentose phosphate (Calvin) cycle in autotrophic metabolism [l]. Among phototrophic purple bacteria the Calvin cycle is universally distributed [l, 21. However, different molecular forms of RuBisCO varying in quaternary structure from the L& green-plant enzyme have been observed in certain species of purple bacteria [l, 21. Among purple sulfur bacteria, RuBisCO from Chromatium vinosum has been particularly well studied, as the native enzyme is an form and can be easily purified and obtained in large amounts [3]. Recent studies of C. vinosum RuBisCO have shown that a catalytically active L8 form of the enzyme can be generated from the native L8S8 form [4]. The ease of obtaining pure preparations of both forms of the enzyme from C. vinosum has focused efforts towards defining the role of small subunits in the overall reaction sequence. Thus far, it appears clear that RuBisCO small subunits have no catalytic functions but may play a regulatory role in promoting activation of the intact enzyme [5, 61. Recently, a thermophilic species of Chromatium, Chromatium tepidurn, was isolated by our laboratory [7,8] and shown to fix CO, via the Calvin cycle [9]. Reflecting its hot-spring origin, C. tepidum was shown to produce a thermally active RuBisCO with a temperature optimum of 50°C [9]. In order to relate these thermal properties to other physical properties Correspondence to M . T. Madigan, Department of Microbiology, Ahhreviations. Ribulose-P,, ribulose-l,5-bisphosphate; RuBisCO, Enzyme. Ribulose-I ,5-bisphosphate carboxylase/oxygenase (EC

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Ribulose 1,5-bisphosphate carboxylase from the thermophilic, acidophilic alga, Cyanidium caldarium (Geitler)

Cited by 34 publications

References 19 publications

Photo- and Metabolite Regulation of the Synthesis of Ribulose Bisphosphate Carboxylase/Oxygenase and the Phycobiliproteins in the Alga Cyanidium caldarium

Photo- and Metabolite Regulation of the Synthesis of Ribulose Bisphosphate Carboxylase/Oxygenase and the Phycobiliproteins in the Alga Cyanidium caldarium

Kinetic properties of ribulose bisphosphate carboxylase/oxygenase from Thiobacillus thyasiris, the putative symbiont of Thyasira flexuosa (Montagu), a bivalve mussel

Purification and characterization of the thermostable ribulose‐1,5‐bisphosphate carboxylase/oxygenase from the thermophilic purple bacterium Chromatium tepidum

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