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. 1980 Mar;77(3):1361–1364. doi: 10.1073/pnas.77.3.1361

Biosynthesis and assembly of the proton-translocating adenosine triphosphatase complex from chloroplasts

Nathan Nelson 1,*, Hannah Nelson 1, Gottfried Schatz 1
PMCID: PMC348494  PMID: 16592786

Abstract

The H+-translocating ATPase complex of chloroplasts consists of at least eight nonidentical subunits. Five of these (α, β, γ, δ, and ε subunits) collectively constitute the globular extramembranous CF1 portion of the complex. The remaining three subunits (I-III) represent the membrane-embedded portion. Biosynthesis and assembly of these subunits were studied by pulse-labeling isolated spinach chloroplasts in the presence of cycloheximide or chloramphenicol and by translating total leaf RNA in a rabbit reticulocyte system. The labeled products were analyzed by immunoprecipitation with subunit-specific antisera or by isolating the entire H+-translocating ATPase complex in a nearly pure state. We found that chloroplasts synthesize the α, β, γ, and ε subunits of CF1, the membrane-embedded subunit I, and probably also the membrane-embedded subunit III. The δ subunit (and probably also subunit II) are imported from the cytoplasm via larger precursor forms. After isolated chloroplasts are labeled in the presence of cycloheximide, the chloroplast-made H+-ATPase subunits are assembled into a complex that is indistinguishable from the authentic H+-ATPase complex. This assembly indicates that isolated chloroplasts contain excess pools of the cytoplasmically made subunits.

Keywords: coupling factor, immunoprecipitation, in vitro synthesis, precursors, assembly

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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