Understanding heterogeneity of eukaryotic chaperonin complex

Protein folding is an important cellular process, and malfunction of protein folding often leads to range of developmental phenotypes, and even diseases. TRiC/CCT chaperonins are conserved throughout eukaryotic species and essential for folding ~10% of protein substrates including actin and tubulin (Smith, Wilardson. 2022). Each chaperonin is composed of two protomers of 8 different subunits, assembling into 16-mer oligomer barrel. Each subunit has the equatorial domain forming the barrel, and the apical domain which provides substrate specificity. In Arabidopsis and other plant species, duplication of these subunit genes is common (Ahn et al. 2019). For example, Arabidopsis has 2 paralogs of CCT6. It is unknown whether these two isoforms are both incorporated into the chaperonin, and have similar roles in folding, or whether they have gained new functions and are involved in folding different substrates at different conditions.

This PhD studentship will focus on investigating the differences of the TRiC/CCT complex in terms of its substrate specificity, and physiological function by incorporation of different paralogs of CCT6. The prospective student will gain experience with biochemical and bioinformatics techniques, including but not limited to protein complex purification followed by IP-MS for substrate specificity and subsequent data analysis, as well as contribute to biological understanding of the roles of protein folding in plants.

Please visit https://plantproteincomplexes.uk for more information about the research focus and publication of the Ahn Lab.

Those interested, please send your CV and Cover letter to [Email Address Removed]