Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
UniProtKB/Swiss-Prot entry P00877 (RBL_CHLRE)
First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii.
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The 1.4 A crystal structure of Chlamydomonas Rubisco shows the L8S8 holoenzyme architecture.
"Overall, the structure shows high similarity to the previously determined structures of L8S8 Rubisco enzymes."
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High-resolution data reveal post-translational modifications, including cysteine methylation and proline 4-hydroxylation.
"These include cysteine and N-terminal methylations and proline 4-hydroxylations."
Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphate.
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The activated Chlamydomonas holoenzyme with the transition-state analogue 2-CABP has the form I L8S8 subunit arrangement.
"The subunit arrangement of Chlamydomonas rubisco is the same as those of the previously solved form I rubiscos."
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Large-subunit active site conformation matches activated spinach Rubisco.
"Especially, the present structure is very similar to the activated spinach structure complexed with 2-CABP in the L-subunit folding and active-site conformation, but differs in S-subunit folding."
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Large subunit carries 4-hydroxyproline at residues 104 and 151 and S-methylcysteine at residues 256 and 369.
"residues 104 and 151 of the L-subunit are 4-hydroxyproline, and residues 256 and 369 of the L-subunit are S(gamma)-methylcysteine."
The intracellular localization of ribulose-1,5-bisphosphate Carboxylase/Oxygenase in chlamydomonas reinhardtii.
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The pyrenoid holds about 90% of Rubisco at ambient CO2 and about 40% at elevated CO2; the rest is in the stroma.
"about 40% was in the pyrenoid when the cells were grown under elevated CO2 and about 90% with ambient CO2."
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Pyrenoidal Rubisco is likely active in CO2 fixation.
"it is likely that pyrenoidal Rubisco is active in CO2 fixation"
Plant-like substitutions in the large-subunit carboxy terminus of Chlamydomonas Rubisco increase CO2/O2 specificity.
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Chlamydomonas Rubisco is L8S8 with chloroplast-encoded rbcL large subunits and nuclear rbcS small subunits; Rubisco-null mutants survive on acetate.
"Mutants that lack Rubisco function can be maintained with acetate"
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Large-subunit carboxy-terminal substitutions introduced by chloroplast transformation of an rbcL deletion strain alter CO2/O2 specificity of the purified enzyme.
"The Ω value of the D470P/T471A/I472M/K474T quadruple-mutant Rubisco enzyme is 10% higher than that of the wild-type Chlamydomonas enzyme."
Functional hybrid rubisco enzymes with plant small subunits and algal large subunits: engineered rbcS cDNA for expression in chlamydomonas.
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The large subunit contains the active site; small subunits modulate catalysis.
"Although the large subunit contains the active site"
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Hybrid Rubisco with plant small subunits and algal large subunits is catalytically proficient but lacks pyrenoids, implicating the small subunit in pyrenoid targeting.
"It appears that small subunits contain the structural elements responsible for targeting Rubisco to the algal pyrenoid"
Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.
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Pyrenoid formation depends on two surface alpha-helices of the small subunit, not on the large subunit.
"Specifically, pyrenoid occurrence was shown to be conditioned by the amino acid composition of two surface-exposed α-helices of the SSU"
The phase separation underlying the pyrenoid-based microalgal Rubisco supercharger.
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Purified Rubisco and EPYC1 phase separate, and condensed Rubisco is catalytically functional.
"The phase-separated Rubisco is functional."
The structural basis of Rubisco phase separation in the pyrenoid.
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EPYC1 binds the Rubisco small subunit, in contrast to carboxysomal linkers that bind between large subunits.
"A notable difference is the location of the binding site on Rubisco: whereas both carboxysomal linker proteins bind to the interface between two Rubisco large subunits24,26, EPYC1 binds to the Rubisco small subunit."
The Eukaryotic CO(2)-Concentrating Organelle Is Liquid-like and Exhibits Dynamic Reorganization.
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The pyrenoid matrix, made largely of Rubisco and EPYC1, behaves like a liquid.
"the internal mixing of matrix components demonstrates that the Chlamydomonas pyrenoid matrix behaves like a liquid."