Homologous plant and bacterial proteins chaperone oligomeric protein assembly View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1988-05

AUTHORS

Sean M. Hemmingsen, Carol Woolford, Saskia M. van der Vies, Kit Tilly, David T. Dennis, Costa P. Georgopoulos, Roger W. Hendrix, R. John Ellis

ABSTRACT

An abundant chloroplast protein is implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase-oxygenase, which catalyses photosynthetic CO2-fixation in higher plants. The product of the Escherichia coli groEL gene is essential for cell viability and is required for the assembly of bacteriophage capsids. Sequencing of the groEL gene and the complementary cDNA encoding the chloroplast protein has revealed that these proteins are evolutionary homologues which we term 'chaperonins'. Chaperonins comprise a class of molecular chaperones that are found in chloroplasts, mitochondria and prokaryotes. Assisted post-translational assembly of oligomeric protein structures is emerging as a general cellular phenomenon. More... »

PAGES

330-334

Journal

TITLE

Nature

ISSUE

6171

VOLUME

333

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/333330a0

DOI

http://dx.doi.org/10.1038/333330a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012301089

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2897629


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