The life of ribulose 1,5-bisphosphate carboxylase/oxygenase - Posttranslational facts and mysteries

Robert L. Houtz, Archie R. Portis

Research output: Contribution to journalShort surveypeer-review

78 Scopus citations

Abstract

The life of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), from gene to protein to irreplaceable component of photosynthetic CO2 assimilation, has successfully served as a model for a number of essential cellular processes centered on protein chemistry and amino acid modifications. Once translated, the two subunits of Rubisco undergo a myriad of co- and posttranslational modifications accompanied by constant interactions with structurally modifying enzymes. Even after final assembly, the essential role played by Rubisco in photosynthetic CO2 assimilation is dependent on continuous conformation modifications by Rubisco activase. Rubisco is also continuously assaulted by various environmental factors, resulting in its turnover and degradation by processes that appear to be enhanced during plant senescence.

Original languageEnglish
Pages (from-to)150-158
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume414
Issue number2
DOIs
StatePublished - Jun 15 2003

Bibliographical note

Funding Information:
This work was supported by U.S. Department of Energy Grants DEFG02-92ER20075 (R.L.H.) and DEAIG2-97ER20268 (A.R.P.).

Keywords

  • Activase
  • Methylation
  • Oxidation
  • Posttranslational
  • Protein folding
  • Ribulose 1,5-bisphosphate
  • Ribulose 1,5-bisphosphate carboxylase/oxygenase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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