Biochemistry: Tackling unintelligent design

@article{Ellis2010BiochemistryTU,
  title={Biochemistry: Tackling unintelligent design},
  author={R. John Ellis},
  journal={Nature},
  year={2010},
  volume={463},
  pages={164-165}
}
  • R. Ellis
  • Published 14 January 2010
  • Computer Science
  • 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

It is demonstrated that the tailored device creates an environment where the enzyme can retain its function while being protected from denaturing conditions and it is envisioned that the 3-PGA produced by RuBisCO will be converted into value-added products.

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
...

References

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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.

Molecular chaperones: assisting assembly in addition to folding.

  • R. Ellis
  • Biology
    Trends in biochemical sciences
  • 2006

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.

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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.