The role of N-terminal post-translational modifications of the tobacco Rubisco large subunit

Understanding the role and function of post translational protein modifications in chloroplasts using the model protein Rubisco.

The co- and post-translational modification of proteins during maturation is an almost ubiquitous process which has long been observed to be essential for protein regulation, activation, and degradation in a large range of organisms. In higher plant chloroplasts Rubisco biogenesis is a highly complex process that necessitates the co-ordinated expression and assembly of its 8 large (L) and 8 small (S) subunits into a hexadecamer (L8S8). The L subunits house the catalytic sites and are subject to the post-translational aminopeptidase removal of Met-1 and Ser-2, and the acetylation of the new N-terminal Pro-3. The function of these modifications are undefined. This research project is focused on improving our fundamental understanding of the function and necessity of the L-subunit co- and post-translational modifications in tobacco chloroplasts. 

Suggested reading

  • Houtz RL, Magnani R, Nayak NR, Dirk LMA (2008) Co- and post-translational modifications in Rubisco: unanswered questions. J Exp Bot 59: 1635-1645


This work is being done in collaboration with Professor Robert Houtz, University of Kentucky (USA).

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