Premium
The transit sequence of a chloroplast precursor protein reorients the lipids in monogalactosyl diglyceride containing bilayers
Author(s) -
Chupin Vladimir,
van't Hof Ron,
de Kruijff Ben
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00734-9
Subject(s) - chloroplast , diglyceride , chemistry , bilayer , biochemistry , phosphatidylcholine , galactolipid , membrane , ferredoxin , diacylglycerol kinase , chloroplast membrane , biophysics , stereochemistry , crystallography , thylakoid , biology , phospholipid , enzyme , gene , protein kinase c
The interaction of the chloroplast precursor protein of ferredoxin with mixed model membranes composed of 2 H chain labeled monogalactosyl diacylglycerol and phosphatidylcholine was studied by 2 H and 31 P NMR. The bilayers were found to have special chain packing properties which most likely are the result of a specific arrangement of head groups at the interface. The precursor and not the corresponding apoprotein induced a bilayer → isotropic transition in lipid organization as a result of the transit sequence—lipid interaction. The implications of these observations for proteins import into chloroplasts are indicated.