The complexity of chloroplast chaperonins

Anna Vitlin Gruber, Shahar Nisemblat, Abdussalam Azem*, Celeste Weiss

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

47 Scopus citations

Abstract

Type I chaperonins are large oligomeric protein ensembles that are involved in the folding and assembly of other proteins. Chloroplast chaperonins and co-chaperonins exist in multiple copies of two distinct isoforms that can combine to form a range of labile oligomeric structures. This complex system increases the potential number of chaperonin substrates and possibilities for regulation. The incorporation of unique subunits into the oligomer can modify substrate specificity. Some subunits are upregulated in response to heat shock and some show organ-specific expression, whereas others possess additional functions that are unrelated to their role in protein folding. Accumulating evidence suggests that specific subunits have distinct roles in biogenesis of ribulose-1,5-bisphosphate carboxylase oxygenase (Rubisco).

Original languageEnglish
Pages (from-to)688-694
Number of pages7
JournalTrends in Plant Science
Volume18
Issue number12
DOIs
StatePublished - Dec 2013

Funding

FundersFunder number
United States - Israel Binational Agricultural Research and Development Fund

    Keywords

    • Chaperone
    • Chaperonin
    • Chloroplast
    • Protein folding
    • Rubisco

    Fingerprint

    Dive into the research topics of 'The complexity of chloroplast chaperonins'. Together they form a unique fingerprint.

    Cite this