Molecular and cellular regulation of autotrophic carbon dioxide fixation in microorganisms.

Tabita, F. Robert

doi:10.1128/mmbr.52.2.155-189.1988

Cited by 159 publications

(108 citation statements)

References 262 publications

(452 reference statements)

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“…Rubisco may represent, depending on growth conditions, between 3% to SO% of the soluble cellular protein on phototrophic bacteria [16]. These values are similar or higher than those obtained after expressing Rubisco in E. coli ( Table 2).…”

Section: Discussionsupporting

confidence: 58%

The 70‐kDa Heat‐Shock Protein/DnaK Chaperone System is Required for the Productive Folding of Ribulose‐Bisphosphate Carboxylase Subunits in Escherichia Coli

Checa

Viale

1997

European Journal of Biochemistry

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We have studied the in vivo requirements of the DnaK chaperone system for the folding of recombinant ribulose-bisphosphate carboxylase/oxygenase in Esc-hrrichia coli. Expression of functional dimeric or hcxadecaineric ribulose-bisphosphate carboxylase from different bacterial sources (including purple bacteria and cyanobacteria) was severely impaired in E. coli dnaK, tltztrJ, or grpE mutants. These enzymes were synthesized mostly in soluble, fully enzymatically active forms in wild-type E. t.o/i cells cultured in the temperature range 20-42"C, but aggregated extensively in rlnaK null mutants. Co-expression of d t u K , but not groESL, markedly reduced the aggregation of ribulose-bisphosphate carboxylase subunits in dnnK null mutants and restored the enzyme activity to levels found in isogenic wild-type strains. Ribulose-bisphosphate carboxylase expression in wild-type E. coli cells growing at 30°C promoted an enhanced synthesis of stress proteins, apparently by sequestering DnaK from its negative regulatory role in this responsc. The overall results indicate that the DnaK chaperone system assists in vivo the folding pathway of ribulose-bisphosphate carboxylase large subunits, most probably at its very early stages.Kepcvords: DnaK ; heat-shock protein (70 kDa) ; in vivo protein folding ; molecular chaperones ; ribulosebisphosphate carboxylase.The observation that purified proteins can refold spontaneously in vitro to their native, three-dimensional conformation has strongly supported the idea that the genetic information required for proper folding is contained i n the polypeptide primary structure [ 1 -41. Nevertheless, at physiological temperatures and thc rclatively elevated concentration of newly synthesized polypeptides found in cells, higher-order aggregation of folding intermediates is likely to be favoured over first-order isomerization reactions that conduce to the native state [ 1-61, Cells have seemingly solved this problem by evolving distinct specialized protein systems, known as molecular chaperones. These proteins interact with different intermediates among the various stages of protein folding, modulating the kinetic partitioning between productive folding and off-pathway reactions [2-61. Molecular chaperones have been shown to play fundamental roles in the folding, assembly, transport, and degradation of cell polypeptides 12-71, Two of the major chaperone systems, ubiquitously distributed among bacterial cells and the oi-ganelles of eukaryotes, are those of the Hsp70 (70-kDa heat-shock proteins, DnaK and its cohorts DnaJ and GrpE in bacteria) and the Hsp60 (60-kDa heatshock proteins, GroEL and its cohort GroES in bacteria) [4, 6, 849presence of Hsp60/GroE chaperonins) or the production of soluble, functional Rubiscos from plant sources in E. coli are still elusive, reflecting our incomplete understanding of all the components involved in the process of Rubisco folding and assembly 117, 181.The use of mutants deficient in components of a particular chaperone system constitutes a powerful tool...

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Section: Discussionsupporting

confidence: 58%

The 70‐kDa Heat‐Shock Protein/DnaK Chaperone System is Required for the Productive Folding of Ribulose‐Bisphosphate Carboxylase Subunits in Escherichia Coli

Checa

Viale

1997

European Journal of Biochemistry

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“…It is a model organism for the study of photosynthesis, carbon fixation and gene regulation (reviewed in Mackenzie et al, 2007). Most strains carry genes for form IC and II RubisCOs (Tabita, 1988). Both are expressed in the absence of organic carbon (Jouanneau and Tabita, 1986), and form IC may be preferentially expressed under low CO 2 conditions (Tabita, 1988).…”

Section: Introductionmentioning

confidence: 99%

“…Most strains carry genes for form IC and II RubisCOs (Tabita, 1988). Both are expressed in the absence of organic carbon (Jouanneau and Tabita, 1986), and form IC may be preferentially expressed under low CO 2 conditions (Tabita, 1988). One R. sphaeroides strain (ATCC17025) has a form IA RubisCO on one of its megaplasmids (Badger and Bek, 2008); the logistics of tripartite RubisCO expression in this strain have not been addressed.…”

Section: Introductionmentioning

confidence: 99%

Isotope discrimination by form IC RubisCO from Ralstonia eutropha and Rhodobacter sphaeroides, metabolically versatile members of ‘Proteobacteria’ from aquatic and soil habitats

Thomas

Boller

Satagopan

et al. 2018

Environmental Microbiology

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Summary RubisCO, the CO2 fixing enzyme of the Calvin–Benson–Bassham (CBB) cycle, is responsible for the majority of carbon fixation on Earth. RubisCO fixes 12CO2 faster than 13CO2 resulting in 13C‐depleted biomass, enabling the use of δ13C values to trace CBB activity in contemporary and ancient environments. Enzymatic fractionation is expressed as an ε value, and is routinely used in modelling, for example, the global carbon cycle and climate change, and for interpreting trophic interactions. Although values for spinach RubisCO (ε = ~29‰) have routinely been used in such efforts, there are five different forms of RubisCO utilized by diverse photolithoautotrophs and chemolithoautotrophs and ε values, now known for four forms (IA, B, D and II), vary substantially with ε = 11‰ to 27‰. Given the importance of ε values in δ13C evaluation, we measured enzymatic fractionation of the fifth form, form IC RubisCO, which is found widely in aquatic and terrestrial environments. Values were determined for two model organisms, the ‘Proteobacteria’ Ralstonia eutropha (ε = 19.0‰) and Rhodobacter sphaeroides (ε = 22.4‰). It is apparent from these measurements that all RubisCO forms measured to date discriminate less than commonly assumed based on spinach, and that enzyme ε values must be considered when interpreting and modelling variability of δ13C values in nature.

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“…As in most autotrophic microorganisms, T. intermedius assimilates carbon dioxide via the Calvin cycle. Analysis of the key enzyme of the cycle, ribulose-l,5-bisphosphate carboxylase/oxygenase (RuBisCO), from a variety of organisms has revealed the presence of two different forms of the enzyme, form I and form II [3]. Form I, characteristic of higher plants and most microorganisms, is composed of eight large and eight small subunits [3].…”

Section: Introductionmentioning

confidence: 99%

“…Analysis of the key enzyme of the cycle, ribulose-l,5-bisphosphate carboxylase/oxygenase (RuBisCO), from a variety of organisms has revealed the presence of two different forms of the enzyme, form I and form II [3]. Form I, characteristic of higher plants and most microorganisms, is composed of eight large and eight small subunits [3]. Form II, composed of 2-6 large subunits, has been demonstrated in a number of phototrophic bacteria and in Thiobacillus denitrificans [3,4].…”

Section: Introductionmentioning

confidence: 99%

Cloning and expression of the ?-ribulose-1,5-bisphosphate carboxylase/oxygenase form II gene from Thiobacillus intermedius in Escherichia coli

Stoner¹

1993

FEMS Microbiology Letters

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Both form I and II ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) genes were detected in Thiobacillus intermedius by heterologous hybridization using specific probes from Anacystis nidulans and Rhodobacter sphaeroides, respectively. However, only the previously reported form I enzyme could be demonstrated in cells grown under a number of different conditions. The reason(s) why the form II gene is not expressed in T. intermedius is/are not clear at this time. The form II gene was isolated from a lambda library by screening with the Rb. sphaeroides probe. A SalI fragment from this clone was ligated into pUC8 and transformed into Escherichia coli DH5 alpha. Subclones pTi20IIA and pTi20IIB representing both orientations relative to the lac promoter were isolated. Low levels of RuBisCO activity were detected in both induced and non-induced pTi20IIA indicating the probable expression from a T. intermedius promoter. Induced pTi20IIB produced much higher levels of enzyme activity. Analysis of cell-free extracts using sucrose density gradients confirmed the expression of a form II RuBisCO similar in size to that found in Rhodobacter capsulatus. Other Calvin cycle genes were not clustered with either the form I or form II genes.

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Molecular and cellular regulation of autotrophic carbon dioxide fixation in microorganisms.

Cited by 159 publications

References 262 publications

The 70‐kDa Heat‐Shock Protein/DnaK Chaperone System is Required for the Productive Folding of Ribulose‐Bisphosphate Carboxylase Subunits in Escherichia Coli

The 70‐kDa Heat‐Shock Protein/DnaK Chaperone System is Required for the Productive Folding of Ribulose‐Bisphosphate Carboxylase Subunits in Escherichia Coli

Isotope discrimination by form IC RubisCO from Ralstonia eutropha and Rhodobacter sphaeroides, metabolically versatile members of ‘Proteobacteria’ from aquatic and soil habitats

Cloning and expression of the ?-ribulose-1,5-bisphosphate carboxylase/oxygenase form II gene from Thiobacillus intermedius in Escherichia coli

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