NDLI: Ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulation factor1 is required for holoenzyme assembly in maize.

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Ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulation factor1 is required for holoenzyme assembly in maize.

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Insight into ribulose 1,5-bis-phosphate carboxylase/oxygenase assembly in maize.

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Ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulation factor1 is required for holoenzyme assembly in maize.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Feiz, Leila Williams-Carrier, Rosalind Wostrikoff, Katia Belcher, Susan Barkan, Alice Stern, David B.
Description	Country affiliation: United States Author Affiliation: Feiz L ( Boyce Thompson Institute for Plant Research, Cornell University, Ithaca, New York 14853, USA.)
Abstract	Most life is ultimately sustained by photosynthesis and its rate-limiting carbon fixing enzyme, ribulose-1,5-bis-phosphate carboxylase/oxygenase (Rubisco). Although the structurally comparable cyanobacterial Rubisco is amenable to in vitro assembly, the higher plant enzyme has been refractory to such manipulation due to poor understanding of its assembly pathway. Here, we report the identification of a chloroplast protein required for Rubisco accumulation in maize (Zea mays), RUBISCO ACCUMULATION FACTOR1 (RAF1), which lacks any characterized functional domains. Maize lines lacking RAF1 due to Mutator transposon insertions are Rubisco deficient and seedling lethal. Analysis of transcripts and proteins showed that Rubisco large subunit synthesis in raf1 plants is not compromised; however, newly synthesized Rubisco large subunit appears in a high molecular weight form whose accumulation requires a specific chaperonin 60 isoform. Gel filtration analysis and blue native gels showed that endogenous and recombinant RAF1 are trimeric; however, following in vivo cross-linking, RAF1 copurifies with Rubisco large subunit, suggesting that they interact weakly or transiently. RAF1 is predominantly expressed in bundle sheath chloroplasts, consistent with a Rubisco accumulation function. Our results support the hypothesis that RAF1 acts during Rubisco assembly by releasing and/or sequestering the large subunit from chaperonins early in the assembly process.
File Format	HTM / HTML
ISSN	10404651
e-ISSN	1531298X
Journal	THE PLANT CELL ONLINE
Issue Number	8
Volume Number	24
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2012-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Botany Holoenzymes Metabolism Plant Proteins Ribulose-bisphosphate Carboxylase Zea Mays Enzymology Alleles Amino Acid Sequence Chloroplast Proteins Genetics Chloroplasts Chromosomes, Plant Dna Transposable Elements Electrophoresis, Polyacrylamide Gel Escherichia Coli Gene Expression Regulation, Plant Genes, Plant Genetic Complementation Test Molecular Chaperones Molecular Sequence Data Protein Interaction Mapping Recombinant Proteins Sequence Alignment Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science

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