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

doi:10.1016/0014-5793(91)81070-O

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 journal › Article › peer-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 language	English (US)
Pages (from-to)	205-209
Number of pages	5
Journal	FEBS Letters
Volume	289
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(91)81070-O
State	Published - Sep 9 1991
Externally published	Yes

Keywords

Electron microscopy
Protein-protein complex
Quaternary structure
Ribulose-1,5-bisphosphate carboxylase (Rubisco)
Rubisco subunit-binding protein

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

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.",

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AU - Tsuprun, V. L.

AU - Boekema, E. J.

AU - Samsonidze, T. G.

AU - Pushkin, A. V.

PY - 1991/9/9

Y1 - 1991/9/9

N2 - 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.

AB - 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.

KW - Electron microscopy

KW - Protein-protein complex

KW - Quaternary structure

KW - Ribulose-1,5-bisphosphate carboxylase (Rubisco)

KW - Rubisco subunit-binding protein

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

Abstract

Keywords

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