Chloroplast import and sequential maturation of pea carbonic anhydrase: the roles of various parts of the transit peptide

FEBS Letters

Pilon, Marinus²  Forsman, Cecilia¹ 

[1] Department of Biochemistry, Umed University, S-901 87 Umeå, Sweden;Dppartment of Molecular Cell Biology, University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands

关键词: Carbonic anhydrase;    Chloroplast;    Transit peptide;    Processing;    CA;    carbonic anhydrase;    Rubisco;    ribulose-1;    5-bisphosphate carboxylase/oxygenase;    cTP;    chloroplast transit peptide;   

DOI  :  10.1016/0014-5793(94)01391-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown