Electron microscopy of the complexes of ribulose-1,5-bisphosphate carboxylase (Rubisco) and Rubisco subunit-binding protein from pea leaves

V.L. Tsuprun, E.J. Boekema, T.G. Samsonidze, A.V. Pushkin

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

The structure of ribulose-1,5-bisphosphate carboxylase (Rubisco) subunit-binding protein and its interaction with pea leaf chloroplast Rubisco were studied by electron microscopy and image analysis. Electron-microscopic evidence for the association of Rubisco subunit-binding protein, consisting of 14 subunits arranged with 72 point group symmetry, and oligomeric (L8S8) Rubisco was obtained.
Original languageEnglish
Pages (from-to)205-209
Number of pages5
JournalFEBS Letters
Volume289
Issue number2
DOIs
Publication statusPublished - 9-Sept-1991

Keywords

  • RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE (RUBISCO)
  • RUBISCO SUBUNIT-BINDING PROTEIN
  • QUATERNARY STRUCTURE
  • PROTEIN-PROTEIN COMPLEX
  • ELECTRON MICROSCOPY
  • RIBULOSE BISPHOSPHATE CARBOXYLASE
  • MOLECULAR CHAPERONES
  • ESCHERICHIA-COLI
  • GROE
  • IDENTIFICATION
  • CHLOROPLASTS
  • MITOCHONDRIA
  • OXYGENASE

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