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Processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts.
Processing of the dual targeted precursor protein of glutathione reductase in mitochondria and chloroplasts.
Determinants for removal and degradation of transit peptides of chloroplast precursor proteins.
Structure and developmental regulation of a wheat gene encoding the major chlorophyll a/b-binding polypeptide.
Stromal processing peptidase binds transit peptides and initiates their ATP-dependent turnover in chloroplasts.
Identification of two structurally related proteins involved in proteolytic processing of precursors targeted to the chloroplast.
A pea antisense gene for the chloroplast stromal processing peptidase yields seedling lethals in Arabidopsis: survivors show defective GFP import in vivo.
Structural properties of the chloroplast stromal processing peptidase required for its function in transit peptide removal.
Mutations at the transit peptide-mature protein junction separate two cleavage events during chloroplast import of the chlorophyll a/b-binding protein.
Identification of domains in an Arabidopsis acyl carrier protein gene promoter required for maximal organ-specific expression.
A chloroplast processing enzyme involved in precursor maturation shares a zinc-binding motif with a recently recognized family of metalloendopeptidases.
A chloroplast processing enzyme functions as the general stromal processing peptidase.
The chlorophyll a/b-binding protein inserts into the thylakoids independent of its cognate transit peptide.
Identification of a chloroplast coenzyme A-binding protein related to the peroxisomal thiolases.
Chloroplast stromal processing peptidase activity is modulated by transit peptide determinants that include inhibitory roles for its N-terminal domain and initial Met.