English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Complex Chaperone Dependence of Rubisco Biogenesis

Wilson, R. H., & Hayer-Hartl, M. (2018). Complex Chaperone Dependence of Rubisco Biogenesis. Biochemistry, 57(23), 3210-3216. doi:10.1021/acs.biochem.8b00132.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0002-7167-B Version Permalink: http://hdl.handle.net/21.11116/0000-0004-038C-B
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Wilson, Robert H.1, Author              
Hayer-Hartl, Manajit2, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

Content

show
hide
Free keywords: RIBULOSE-BISPHOSPHATE CARBOXYLASE; BUNDLE-SHEATH DEFECTIVE2; ESCHERICHIA-COLI; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; THERMOSYNECHOCOCCUS-ELONGATUS; HEXADECAMERIC RUBISCO; ASSEMBLY CHAPERONE; CRYSTAL-STRUCTURE; PEA-CHLOROPLASTS; LARGE SUBUNITSBiochemistry & Molecular Biology;
 Abstract: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), a similar to 530 kDa complex of 8 large (RbcL) and 8 small subunits (RbcS), mediates the fixation of atmospheric CO2 into usable sugars during photosynthesis. Despite its fundamental role, Rubisco is a remarkably inefficient enzyme and thus is produced by plants in huge amounts. It has long been a key target for bioengineering with the goal to increase crop yields. However, such efforts have been hampered by the complex requirement of Rubisco biogenesis for molecular chaperones. Recent studies have identified an array of auxiliary factors needed for the folding and assembly of the Rubisco subunits. The folding of plant RbcL subunits is mediated by the cylindrical chloroplast chaperonin, Cpn60, and its cofactor Cpn20. Folded RbcL requires a number of additional Rubisco specific assembly chaperones, including RbcX, Rubisco accumulation factors 1 (Raf1) and 2 (Raf2), and the Bundle sheath defective-2 (BSD2), to mediate the assembly of the RbcL, intermediate complex. Incorporation of the RbcS and displacement of the assembly factors generates the active holoenzyme. An Escherichia coli strain expressing the chloroplast chaperonin and auxiliary factors now allows the expression of functional plant Rubisco, paving the way for Rubisco engineering by large scale mutagenesis. Here, we review our current understanding on how these chaperones cooperate to produce one of the most important enzymes in nature.

Details

show
hide
Language(s): eng - English
 Dates: 2018
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: 1155 16TH ST, NW, WASHINGTON, DC 20036 USA : AMER CHEMICAL SOC
Pages: - Volume / Issue: 57 (23) Sequence Number: - Start / End Page: 3210 - 3216 Identifier: ISSN: 0006-2960