Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes.
Chloroplasts consist of six morphologically distinct compartments. Each compartment has a specific set of polypeptides that perform distinct biochemical functions. We report here the identification of a membrane-associated protein with a novel localization. This protein was synthesized as a 37 kDa precursor and was processed to a mature protein of 30 kDa after being imported into isolated pea chloroplasts. Fractionation of chloroplasts showed that the 30 kDa mature protein was associated with both of the envelope membranes as well as with thylakoid membranes. Immunocyto-chemical localization of the 30 kDa protein revealed that the protein occurred in clusters in the vicinity of both the envelope and the thylakoid. Possible functions of this 30 kDa protein, inferred from its novel localization pattern, are discussed.
Li
H M
HM
Department of Botany, University of Wisconsin, Madison 53706.
Kaneko
Y
Y
Keegstra
K
K
D000595:Amino Acid Sequence; D001483:Base Sequence; D002736:Chloroplasts / Q000378:metabolism*; D003001:Cloning, Molecular / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000166:cytology / Q000378:metabolism* / Q000648:ultrastructure; D007150:Immunohistochemistry; D007425:Intracellular Membranes / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000032:analysis / Q000096:biosynthesis* / Q000302:isolation & purification; D010946:Plants, Medicinal
D010940:Plant Proteins