[82] Ribulose-1,5-bisphosphate car☐ylase/oxygenase from spinach, tomato, or tobacco leaves

McCurry, Stephen D.; Gee, Robert; Tolbert, N. E.

doi:10.1016/s0076-6879(82)90178-1

Cited by 61 publications

(48 citation statements)

References 14 publications

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“…8 and 17. Rubisco was purified from spinach or tobacco leaves (28). Kinetic enzyme assays used previously determined conditions, which were optimized for linearity with time and enzyme concentration (18).…”

Section: Methodsmentioning

confidence: 99%

Rubisco in complex with Rubisco large subunit methyltransferase

Raunser

Magnani

Huang

et al. 2009

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

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SET domain protein lysine methyltransferases (PKMT) are a structurally unique class of enzymes that catalyze the specific methylation of lysine residues in a number of different substrates. Especially histone-specific SET domain PKMTs have received widespread attention because of their roles in the regulation of epigenetic gene expression and the development of some cancers. Rubisco large subunit methyltransferase (RLSMT) is a chloroplastlocalized SET domain PKMT responsible for the formation of trimethyl-lysine-14 in the large subunit of Rubisco, an essential photosynthetic enzyme. Here, we have used cryoelectron microscopy to produce an 11-Å density map of the Rubisco-RLSMT complex. The atomic model of the complex, obtained by fitting crystal structures of Rubisco and RLSMT into the density map, shows that the extensive contact regions between the 2 proteins are mainly mediated by hydrophobic residues and leucine-rich repeats. It further provides insights into potential conformational changes that may occur during substrate binding and catalysis. This study presents the first structural analysis of a SET domain PKMT in complex with its intact polypeptide substrate.electron microscopy ͉ LSMT ͉ SET domain ͉ single particle S ET [SU(VAR)3-9, E(Z), and TRX] domain protein lysine methyltransferases (PKMTs) are a structurally unique class of enzymes that catalyze the formation of site-specific methylated lysine residues in a number of different polypeptide substrates including cytochrome c (1, 2), histones (3), ribosomal proteins (3, 4), p53 (5), TAF10 (6), ␥-tocopherol methyltransferase (7), and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) (8). All SET domain PKMTs have a unique and conserved structural motif that contains separate binding sites for the target protein substrate and the methyl donor, Sadenosylmethionine (AdoMet) (9). The mechanisms by which these enzymes achieve site-specific methylation is of great interest and histone-specific SET domain protein methyltransferases (HKMTs) have received widespread attention because of their roles in the regulation of epigenetic gene expression and the development of some cancers (9, 10). The specificity of several SET domain PKMTs has been examined through structural and biochemical analyses of ternary complexes with bound polypeptide substrates, but all of these studies used short synthetic polypeptide mimetics of the intact polypeptide substrate and therefore do not account for the potential influence of areas outside the immediate residues flanking the target lysine methylation site (11)(12)(13)(14)(15)(16). Rubisco large subunit methyltransferase (RLSMT) is a chloroplast-localized SET domain PKMT responsible for the formation of trimethyl-lysine-14 in the large subunit of Rubisco (8,17), an essential photosynthetic enzyme with a hexadecameric structure and large molecular mass (Ϸ534 kDa). Detailed information is available regarding the structure, catalytic mechanism, active site residues, and the kinetic reaction mechanism for pea RLSMT (7,8,17,18)...

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Section: Methodsmentioning

confidence: 99%

Rubisco in complex with Rubisco large subunit methyltransferase

Raunser

Magnani

Huang

et al. 2009

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

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“…RuBP was synthesized as previously described (2 ( 11) and by rocket immunoelectrophoresis (6). Over 90% of the protein in the pooled tubes fractionated from chloroplast extracts was Rubisco.…”

Section: Materials and Methods Materialsmentioning

confidence: 99%

Status of the Substrate Binding Sites of Ribulose Bisphosphate Carboxylase as Determined with 2-C-Carboxyarabinitol 1,5-Bisphosphate

Zhu¹,

Jensen²

1990

Plant Physiol.

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“…In C3 plants, such as spinach, pea, and soybean, the determined Rubisco content may guarantee the photosynthetic rate at 800 to 900 ,umol CO2 fixed mg-' Chl h-', provided that the specific activity of the enzyme is 2.2 ,gmol mg-' Rubisco min-' (18). Comparison of the predicted CO2 fixation rate with the actual photosynthetic rate of leaves indicates that Rubisco participates in photosynthesis with 25 to 30% of its full activity even in the presence of saturating CO2 and light in these plants.…”

Section: Methodsmentioning

confidence: 99%

“…Rather than precipitating the ['4C]CPBP-Rubisco complex with antibody (9), we describe in this paper a modification of the method using PEG-4000 (18) to precipitate the complex. The concentration of binding sites and hence the amount of Rubisco can be determined in a few hours.…”

mentioning

confidence: 99%

Ribulose Bisphosphate Carboxylase/Oxygenase Content Determined with [¹⁴C]Carboxypentitol Bisphosphate in Plants and Algae

Yokota¹,

Canvin²

1985

Plant Physiol.

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[82] Ribulose-1,5-bisphosphate car☐ylase/oxygenase from spinach, tomato, or tobacco leaves

Cited by 61 publications

References 14 publications

Rubisco in complex with Rubisco large subunit methyltransferase

Rubisco in complex with Rubisco large subunit methyltransferase

Status of the Substrate Binding Sites of Ribulose Bisphosphate Carboxylase as Determined with 2-C-Carboxyarabinitol 1,5-Bisphosphate

Ribulose Bisphosphate Carboxylase/Oxygenase Content Determined with [¹⁴C]Carboxypentitol Bisphosphate in Plants and Algae

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[82] Ribulose-1,5-bisphosphate car☐ylase/oxygenase from spinach, tomato, or tobacco leaves

Cited by 61 publications

References 14 publications

Rubisco in complex with Rubisco large subunit methyltransferase

Rubisco in complex with Rubisco large subunit methyltransferase

Status of the Substrate Binding Sites of Ribulose Bisphosphate Carboxylase as Determined with 2-C-Carboxyarabinitol 1,5-Bisphosphate

Ribulose Bisphosphate Carboxylase/Oxygenase Content Determined with [14C]Carboxypentitol Bisphosphate in Plants and Algae

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Ribulose Bisphosphate Carboxylase/Oxygenase Content Determined with [¹⁴C]Carboxypentitol Bisphosphate in Plants and Algae