publication . Article . 2013

Insights into eukaryotic Rubisco assembly : crystal structures of RbcX chaperones from Arabidopsis thaliana

Piotr Kolesinski; Przemyslaw Golik; Przemyslaw Grudnik; Janusz Piechota; Michal Markiewicz; Miroslaw Tarnawski; Grzegorz Dubin; Andrzej Szczepaniak;
Open Access Polish
  • Published: 04 Jan 2013
  • Country: Poland
Abstract
article Background: Chloroplasts were formed by uptake of cyanobacteria into eukaryotic cells ca. 1.6 billion years ago. During evolution most of the cyanobacterial genes were transferred from the chloroplast to the nuclear genome. The rbcX gene, encoding an assembly chaperone required for Rubisco biosynthesis in cyanobacteria, was duplicated. Here we demonstrate that homologous eukaryotic chaperones (AtRbcX1 and AtRbcX2) dem- onstrate different affinities for the C-terminus of Rubisco large subunit and determine their crystal structures. Methods: Three-dimensional structures of AtRbcX1 and AtRbcX2 were resolved by the molecular replacement method. Equilibrium b...
Persistent Identifiers
Subjects
Medical Subject Headings: food and beverages
free text keywords: RbcX, Rubisco assembly, Arabidopsis thaliana, Chloroplast, Biochemistry, Peptide sequence, Molecular replacement, Botany, RuBisCO, biology.protein, biology, Gene, Nuclear gene, Chaperone (protein), Arabidopsis thaliana, biology.organism_classification
Related Organizations
Funded by
EC| PCUBE
Project
PCUBE
Infrastructure for Protein Production Platforms
  • Funder: European Commission (EC)
  • Project Code: 227764
  • Funding stream: FP7 | SP4 | INFRA
Communities
Instruct-ERICInstruct-ERIC Projects: Infrastructure for Protein Production Platforms
Abstract
article Background: Chloroplasts were formed by uptake of cyanobacteria into eukaryotic cells ca. 1.6 billion years ago. During evolution most of the cyanobacterial genes were transferred from the chloroplast to the nuclear genome. The rbcX gene, encoding an assembly chaperone required for Rubisco biosynthesis in cyanobacteria, was duplicated. Here we demonstrate that homologous eukaryotic chaperones (AtRbcX1 and AtRbcX2) dem- onstrate different affinities for the C-terminus of Rubisco large subunit and determine their crystal structures. Methods: Three-dimensional structures of AtRbcX1 and AtRbcX2 were resolved by the molecular replacement method. Equilibrium b...
Persistent Identifiers
Subjects
Medical Subject Headings: food and beverages
free text keywords: RbcX, Rubisco assembly, Arabidopsis thaliana, Chloroplast, Biochemistry, Peptide sequence, Molecular replacement, Botany, RuBisCO, biology.protein, biology, Gene, Nuclear gene, Chaperone (protein), Arabidopsis thaliana, biology.organism_classification
Related Organizations
Funded by
EC| PCUBE
Project
PCUBE
Infrastructure for Protein Production Platforms
  • Funder: European Commission (EC)
  • Project Code: 227764
  • Funding stream: FP7 | SP4 | INFRA
Communities
Instruct-ERICInstruct-ERIC Projects: Infrastructure for Protein Production Platforms
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