Chloroplasts can accommodate inclusion bodies. Evidence from a mutant of Chlamydomonas reinhardtii defective in the assembly of the chloroplast ATP synthase.

doi:10.1074/jbc.270.25.15299

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Article

Chloroplasts can accommodate inclusion bodies. Evidence from a mutant of Chlamydomonas reinhardtii defective in the assembly of the chloroplast ATP synthase.

The Journal of biological chemistry - 23 Jun 1995

Ketchner S L, Drapier D, Olive J, Gaudriault S, Girard-Bascou J, Wollman F A

Abstract excerpt

We identified two neighboring missense mutations in the chloroplast atpA gene which are responsible for the defect of ATP synthase assembly in the FUD16 mutant from Chlamydomonas reinhardtii. The two corresponding amino acid substitutions, Ile184-->Asn and Asn186-->Tyr, occurred at strictly conserved sites among the alpha and beta subunits of (C)F1 complexes from bacteria, mitochondria, and chloroplasts. The...

Topics

Amino Acid Sequence
Animals
Asparagine
Base Sequence
Centrifugation, Density Gradient
Chlamydomonas reinhardtii
Chloroplasts
Conserved Sequence
Crosses, Genetic
Genes, Fungal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Immunohistochemistry

Inclusion Bodies

Isoleucine

Macromolecular Substances

Molecular Sequence Data

Phenotype

Point Mutation

Proton-Translocating ATPases

Source

Open in PubMed

Identifiers

PMID: 7797517
DOI: 10.1074/jbc.270.25.15299

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7797517-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Chloroplasts can accommodate inclusion bodies. Evidence from a mutant of Chlamydomonas reinhardtii defective in the assembly of the chloroplast ATP synthase.PMID 7797517Read ↗

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