Biochemistry: Tackling unintelligent design

  title={Biochemistry: Tackling unintelligent design},
  author={R. John Ellis},
  • R. Ellis
  • Published 14 January 2010
  • Biology, Medicine
  • Nature
The key enzyme in photosynthesis, Rubisco, is a relic of a bygone age. The ability to assemble Rubisco in the test tube offers the prospect of genetically manipulating the enzyme to make it fit for the modern world. 
Role of auxiliary proteins in Rubisco biogenesis and function
An integrated view of the pathways underlying Rubisco biogenesis and repair will pave the way for efforts to improve the enzyme with the goal of increasing crop yields.
Role of the small subunit of Rubisco in the green algal phylogeny and Carbon Concentrating Mechanism expression
Natural Environment Research Council (grant number NE/L002507/1 to Howard Griffiths) and resources associated with BBSRC-BB/M007693/1, BB/I024518/1 as part of the Combining Algal and Plant
Structure and mechanism of the Rubisco-assembly chaperone Raf1
The role of Rubisco accumulation factor1 (Raf1), a dimer of ∼40-kDa subunits, is analyzed and it is found that Raf1 from Synechococcus elongatus acts downstream of chaperonin-assisted RBCL folding by stabilizing RbcL antiparallel dimers for assembly into RbcS8 complexes with four Raf1 dimers bound.
Engineering photorespiration: current state and future possibilities.
An overview about the major current attempts to reduce photorespiratory losses in crop species and suggestions for future research priorities are presented.
Isolation and kinetic characterisation of hydrophobically distinct populations of form I Rubisco
It is demonstrated here that HIC can be employed to isolate form I Rubisco with purities and activities comparable to those obtained via ion exchange chromatography (IEC).
Polypyrrole membranes as scaffolds for biomolecule immobilization
Enzymes have evolved over hundreds of years through changes in ecosystems (climate, atmosphere, hydrology, etc). The evolutionary changes driven by the need to survive has led to enzymes with diverse
The physiology of alien chloroplasts: light adaptation mechanisms in cytoplasmic hybrids of the Solanaceae family.
The investigation presented here is of a new plant model for photosynthesis research which was engineered to contain the nuclear genome of Nicotiana tabacum and the chloroplast genome of Hyoscyamus niger and finds the ability of the Nt(Hn) cybrid to adjust to high and low intensity light environments in terms of acclimation at the level of the whole plant, leaf, tissue, cell, chloropine, pigment, and electron transport rates.
Investigation of carbon and energy metabolic mechanism of mixotrophy in Chromochloris zofingiensis
The photosynthesis rate-limiting enzyme, RuBisCO, was skipped in mixotrophy, which could reduce energy waste of photosynthesis while promote cell growth, and provides a foundation for future studies on mixotrophic biomass production and photosynthetic metabolism.
Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
As the global atmospheric emissions of carbon dioxide (CO2) and other greenhouse gases continue to grow to record-setting levels, so do the demands for an efficient and inexpensive carbon
CO2-capture by engineered mammalian carbonic anhydrases
Abstract The favorable characteristics of carbonic anhydrases (CAs) for the efficient and selective capture of CO2 have made them attractive candidates for numerous environmental, industrial, and


Rubisco: structure, regulatory interactions, and possibilities for a better enzyme.
The interactions and associations relatively far from the Rubisco active site, including regulatory interactions with Rubisco activase, may present new approaches and strategies for understanding and ultimately improving this complex enzyme.
Coupled chaperone action in folding and assembly of hexadecameric Rubisco
It is shown that RbcL subunit folding by the GroEL/GroES chaperonin is tightly coupled with assembly mediated by the chaperone RbcX2, and specific assembly chaperones may be required more generally in the formation of complex oligomeric structures when folding is closely coupled to assembly.
Structure and Function of RbcX, an Assembly Chaperone for Hexadecameric Rubisco
The role of RbcX is described as an assembly chaperone of ribulose-bisphosphate carboxylase/oxygenase (Rubisco), the enzyme responsible for the fixation of atmospheric carbon dioxide.
Molecular chaperones: assisting assembly in addition to folding.
  • R. Ellis
  • Biology, Medicine
    Trends in biochemical sciences
  • 2006
The common perception that molecular chaperones are involved primarily with assisting the folding of newly synthesized and stress-denatured polypeptide chains ignores the fact that this term was
Converging concepts of protein folding in vitro and in vivo
Recent concepts emerging from studies of protein folding in vitro and in vivo are reviewed, with a focus on how proteins navigate the complex folding energy landscape inside cells with the aid of molecular chaperones.
Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts.
Results indicate assembly of large subunits into ribulose bisphosphate carboxylase in the sorbitol medium and time course experiments indicate that there is a time-lag of several minutes between onset of synthesis of largeSubunits and the onset of assembly.
Protein aggregation in crowded environments
The quantitative effects of crowding on protein aggregation and the role of molecular chaperones in combating this problem are discussed.
Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
The nucleosome assembly protein has been identified and purified from eggs of Xenopus laevis and it is shown that it binds histones and DNA to form nucleosomes.
Proteins as molecular chaperones