Chloroplast import and sequential maturation of pea carbonic anhydrase: the roles of various parts of the transit peptide.
Chloroplast pea carbonic anhydrase is synthesised in the cytosol with an unusually long bipartite N-terminal extension of the mature sequence previously proposed to serve as a transit peptide. Studies of import into pea chloroplasts show that the N-terminal 69 amino acids of the previously proposed transit peptide is sufficient for translocation and localisation to the stroma, while the acidic C-terminal part does not seem to have any function in these processes. Processing of the in vitro imported precursors is shown to be at a new cleavage site located in the middle of the actual transit peptide. The results indicate that maturation occurs in more than one step. The time-course does not seem to be dependent on the age of the chloroplast but on the age of the translocated precursor.
Forsman
C
C
Department of Biochemistry, Umeå University, Sweden.
Pilon
M
M
D002256:Carbonic Anhydrases / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism*; D018532:Pisum sativum / Q000201:enzymology*; D018515:Plant Leaves / Q000737:chemistry; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000235:genetics / Q000378:metabolism*; D017384:Sequence Deletion / Q000502:physiology
D011498:Protein Precursors; D021382:Protein Sorting Signals; D002256:Carbonic Anhydrases