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Characterization of thylakoid-derived lipid-protein particles bearing the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase

Author:
Smith, M.D., Ghosh, S., Dumbroff, E.B., Thompson, J.E.
Source:
Plant physiology 1997 v.115 no.3 pp. 1073-1082
ISSN:
0032-0889
Subject:
ribulose-bisphosphate carboxylase, fatty acids, thylakoids, proteinases, adenosine triphosphate, Phaseolus vulgaris, esters, light, chemical constituents of plants, protein content, enzyme activity
Abstract:
Lipid-protein particles bearing the 55-kD ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) (EC 4.1.1.39) large subunit (RLSU) and no detectable corresponding Rubisco small subunit (RSSU) were isolated from the stroma of intact chloroplasts by flotation centrifugation. Stromal RLSU-bearing particles appear to originate from thylakoids because they can also be generated in vitro by illumination of isolated thylakoids. Their formation in vitro is largely heat denaturable and is facilitated by light or ATP. RLSU-containing lipid-protein particles range from 0.05 to 0.10 micrometers in radius, contain the same fatty acids as thylakoids, but have a 10- to 15-fold higher free-to-esterified fatty acid ratio than thylakoids. RLSU-bearing lipid-protein particles with no detectable RSSU were also immunopurified from the populations of both stromal lipid-protein particles and those generated in vitro from illuminated thylakoids. Protease shaving indicated that the RLSU is embedded in the lipid-protein particles and that there is also a protease-protected RLSU in thylakoids. These observations collectively indicate that the RLSU associated with thylakoids is released into the stroma by light-facilitated blebbing of lipid-protein particles. The release of RLSU-containing particles may in turn be coordinated with the assembly of Rubisco holoenzyme because chaperonin 60 is also associated with lipid-protein particles isolated from stroma.
Agid:
665259