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Protein Complexes with Interchangeable Parts

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Related Experiment Video

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The MultiBac Protein Complex Production Platform at the EMBL

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Multiple Rieske/cytb complexes in a single organism.

F ten Brink¹, B Schoepp-Cothenet, R van Lis

¹BIP/UMR7281, FR3479, CNRS/AMU, 13 chemin Joseph Aiguier, 13009 Marseille, France.

Biochimica Et Biophysica Acta

|March 20, 2013

Summary

This summary is machine-generated.

Many organisms possess multiple copies of the Rieske/cytochrome b (cytb) complex, an essential enzyme in electron transfer chains. This review explores the distribution and specialized functions of these redundant complexes across diverse species.

Keywords:

Bioenergetics Energy conservation Energy metabolism Evolution Quinone Rieske/cytb complex

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Area of Science:

Biochemistry
Molecular Biology
Microbiology

Background:

The Rieske/cytochrome b (cytb) complex is a crucial component of respiratory and photosynthetic electron transfer chains.
While typically present as a single copy, multiple copies of this complex are found in various phylogenetically distant organisms.
The functional significance of this redundancy remains largely unexplained.

Purpose of the Study:

To review the distribution of multiple Rieske/cytb complex copies across different species.
To analyze the properties and potential functions of these redundant complexes.
To propose future research directions for understanding their roles.

Main Methods:

Compilation and analysis of existing experimental data.
Bioinformatic analysis of amino acid sequences.
Examination of genomic context for duplicated genes.

Main Results:

Identified specialized functions for duplicated Rieske/cytb complexes, including reverse electron transfer in iron-oxidizing bacteria.
Observed adaptation of multiple copies for interaction with different oxidases in archaeal Thermoprotei.
Noted the import of a second complex with a putative heme c(i) in several species, suggesting novel properties.

Conclusions:

Multiple copies of the Rieske/cytb complex are not merely redundant but appear to be functionally specialized.
Specific adaptations suggest roles in unique metabolic strategies, such as acidophilic iron oxidation and diverse electron acceptors.
Further research is needed to elucidate the precise functions and evolutionary advantages of these duplicated complexes.