Co- and post-translational modifications in Rubisco: Unanswered questions

Robert L. Houtz, Roberta Magnani, Nihar R. Nayak, Lynnette M.A. Dirk

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

Both the large (LS) and small (SS) subunits of Rubisco are subject to a plethora of co- and post-translational modifications. With the exceptions of LS carbamylation and SS transit sequence processing, the remaining modifications, including deformylation, acetylation, methylation, and N-terminal proteolytic processing of the LS, are still biochemically and/or functionally undefined although they are found in nearly all forms of Rubisco from vascular plants. A collection of relatively unique enzymes catalyse these modifications, and several have been characterized in other organisms. Some of the observed modifications in the LS and SS clearly suggest novel changes in enzyme specificity and/or activity, and others have common features with other co- and post-translationally modifying enzymes. With the possible exception of Lys14 methylation in the LS, processing of both the LS and SS of Rubisco is by default an ordered process sequentially leading up to the final forms observed in the holoenzyme. An overview of the nature of structural modifications in the LS and SS of Rubisco is presented, and, where possible, the nature of the enzymes catalysing these modifications (either through similarity with other known enzymes or through direct enzymological characterization) is described. Overall, there are a distinct lack of functional and mechanistic observations for modifications in Rubisco and thus represent many potentially productive avenues for research.

Original languageEnglish
Pages (from-to)1635-1645
Number of pages11
JournalJournal of Experimental Botany
Volume59
Issue number7
DOIs
StatePublished - May 2008

Bibliographical note

Funding Information:
Our thanks for technical efforts for confocal imaging go to Dr Randy D Dinkins, Research Plant Molecular Geneticist at USDA/ ARS in the Forage Animal Production Research Unit. We also acknowledge Dr Brent W Meier for contributing the demonstration of the activity of the Arabidopsis Rubisco LSMT. This work was supported by the Department of Energy grant (#DE-FG02-92ER20075) to RLH.

Keywords

  • Co-translational processing
  • Dipeptidase
  • Methionine aminopeptidase
  • N- acetyltransferase
  • N- methyltransferase
  • Peptide deformylase
  • Post-translational processing
  • Rubisco
  • Stromal processing peptidase

ASJC Scopus subject areas

  • Physiology
  • Plant Science

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