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A functionally active protein import complex from
Author(s) -
Soil Jürgen,
Waegemann Karin
Publication year - 1992
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/j.1365-313x.1992.00253.x
Subject(s) - digitonin , membrane , protease , biophysics , chemistry , biochemistry , chloroplast , enzyme , biology , gene
Isolated outer chloroplast envelope membranes were solubilized by digitonin and separated on linear sucrose density gradients. A membrane complex was recovered from the gradients and exhibited characteristics of a protein import apparatus, i.e. the interaction of the complex with the precursor polypeptides depends on the presence of a transit sequence, ATP and protease‐sensitive components. Furthermore, trans‐location intermediates detected in the organellar system are also found after interaction of the precursor polypeptide with the isolated import complex.