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

  • Robert L. Houtz
  • , Archie R. Portis

Producción científica: Short survey › revisión exhaustiva

82 Citas (Scopus)

Resumen

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.

Idioma originalEnglish
Páginas (desde-hasta)150-158
Número de páginas9
PublicaciónArchives of Biochemistry and Biophysics
Volumen414
N.º2
DOI
EstadoPublished - jun 15 2003

Nota bibliográfica

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

Financiación

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

FinanciadoresNúmero del financiador
Michigan State University-U.S. Department of Energy (MSU-DOE) Plant Research LaboratoryDEAIG2-97ER20268, DEFG02-92ER20075

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology

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