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PMID: 6725425 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

ATP-released large subunits participate in the assembly of RuBP carboxylase.

Journal of cellular biochemistry ·Vol. 24 ·No. 2 ·1984-00-00 ·Pages 153-62

Milos P, Roy H

Abstract

Preincubation of 35S-methionine-labeled chloroplast extracts with ATP at 0 degree C potentiates the subsequent assembly of labeled large subunits into RuBPCase . This is correlated with the dissociation of newly synthesized large subunits from the 29S large subunit binding protein complex. These released large subunits then assemble into RuBPCase in a second, nucleotide-stimulated reaction. The data demonstrate that the 29S complex can play an active role in the assembly of RuBPCase .

MeSH Terms
Adenosine Triphosphate/physiology Chloroplasts/metabolism Densitometry Electrophoresis, Polyacrylamide Gel Plant Proteins/biosynthesis Plants/metabolism Ribulose-Bisphosphate Carboxylase/metabolism
Chemicals
Plant Proteins Adenosine Triphosphate Ribulose-Bisphosphate Carboxylase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Milos P
Roy H
Article Info
Journal
Journal of cellular biochemistry
Abbr.
J Cell Biochem
ISSN
0730-2312
Published
1984-00-00
Pages
153-62
Language
English
Region
United States
NLM ID
8205768
Subset
IM
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