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Literature summary extracted from

  • Muto, M.; Henry, R.E.; Mayfield, S.P.
    Accumulation and processing of a recombinant protein designed as a cleavable fusion to the endogenous Rubisco LSU protein in Chlamydomonas chloroplast (2009), BMC Biotechnol., 9, 26.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.1.1.39 biotechnology it is examined if recombinant protein accumulation can be enhanced by genetically fusing the recombinant reporter protein, luciferase, to the carboxy-terminal end of an abundant endogenous protein, the large subunit of ribulose bisphosphate carboxylase. A native protein-processing site from preferredoxin (preFd) is placed between the Rubisco LSU and luciferase coding regions in the fusion protein construct. Results demonstrate the utility of using fusion proteins to enhance recombinant protein accumulation in algal chloroplasts, and also show that engineered proteolytic processing sites can be used to liberate the exogenous protein from the endogenous fusion partner, allowing for the purification of the intended mature protein Chlamydomonas reinhardtii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.1.39 chloroplast
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 Chlamydomonas reinhardtii 9507
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Organism

EC Number Organism UniProt Comment Textmining
4.1.1.39 Chlamydomonas reinhardtii
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-
-

Synonyms

EC Number Synonyms Comment Organism
4.1.1.39 ribulose bisphosphate carboxylase
-
 Chlamydomonas reinhardtii
4.1.1.39 Rubisco-LSU
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 Chlamydomonas reinhardtii