FEBS Letters · 1998 · 105 citations · 24 references
Life SciencesPlant BiologyPlant SciencesPlant BiochemistryPlant Molecular BiologyProtein TranslationChloroplast BiochemistryChloroplast BiologyChloroplast StructureChloroplast Membrane Protein ComplexesChloroplast Protein ImportMembrane Protein ImportPrecursor Protein MaturationProtein Translocation Across The Chloroplast EnvelopeProteolytic ActivitySubunit Assembly
The protein import complex of the chloroplastic outer envelope (Toc-complex) contains a prominent subunit of 86 kDa molecular weight (Toc86). Toc86 was identified as a putative precursor receptor. The Arabidopsis genome sequencing project indicates that Toc86 represents only a proteolytic fragment of a larger polypeptide of 160 kDa. The 160-kDa protein, which we name Toc160, is only present in significant amounts in pea chloroplasts isolated under stringent conditions. The capacity of chloroplasts to import an in vitro translated precursor protein correlates well with the integrity of Toc160. We conclude that Toc160 is still a bonafide subunit of the protein import machinery of chloroplasts.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN <i>BETA VULGARIS</i>
Daniel I. Arnon · PLANT PHYSIOLOGY · 1949 · 22.3K citations · Full text