Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species

Robert L. Houtz, Loelle Poneleit, Samantha B. Jones, Malcolm Royer, John T. Stults

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

A combination of limited tryptic proteolysis, reverse phase-high performance liquid chromatography, Edman degradative sequencing, amino acid analysis, and fast-atom bombardment mass-spectrometry was used to remove and identify the first 14 to 18 N-terminal amino acid residues of the large subunit of higher plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Chlamydomonas reinhardtii, Marchantia polymorpha, pea (Pisum sativum), tomato (Lycopersicon esculentum), potato (Solarium tuberosum), pepper (Capsicum annuum), soybean (Glycine max), petunia (Petunia x hybrids), cowpea (Vigna sinensis), and cucumber (Cucumis sativus) plants. The N-terminal tryptic peptide from acetylated Pro-3 to Lys-8 of the large subunit of Rubisco was identical in all species, but the amino acid sequence of the penultimate N-terminal tryptic peptide varied. Eight of the 10 species examined contained a trimethyllysyl residue at position 14 in the large subunit of Rubisco, whereas Chlamydomonas and Marchantia contained an unmodified lysyl residue at this position.

Original languageEnglish
Pages (from-to)1170-1174
Number of pages5
JournalPlant Physiology
Volume98
Issue number3
DOIs
StatePublished - 1992

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science

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