Expression and purification of the mitochondrial uncoupling proteins: a comparative study between Escherichia coli and Saccharomyces cerevisiae

Specific antibodies directed against Drosophila melanogaster acidic ribosomal protein S14 were used in a comparative study of eucaryotic and procaryotic ribosomes by immunoblotting and enzyme-linked immunosorbent assays. Common antigenic determinants and, thus, structural homology were found between D. melanogaster, Saccharomyces cerevisiae (S25), rabbit liver (S12), Bacillus subtilis (S6), and Escherichia coli (S6) ribosomes.

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Mitochondrial Uncoupling Proteins in Mammals and Plants

Bioscience Reports ◽

10.1023/a:1013604526175 ◽

2001 ◽

Vol 21 (2) ◽

pp. 201-212 ◽

Cited By ~ 44

Author(s):

Jirí Borecký ◽

Ivan G. Maia ◽

Paulo Arruda

Keyword(s):

Uncoupling Protein ◽

Uncoupling Proteins ◽

Mitochondrial Uncoupling ◽

Anion Transporter ◽

Distinct Cluster ◽

Mitochondrial Uncoupling Proteins ◽

Shivering Thermogenesis ◽

General Balance ◽

Anion Carrier

Uncoupling proteins (UCPs) belong to a distinct cluster of the mitochondrial anion carrier family. Up to five different uncoupling protein types were found in mitochondria of mammals and plants, and recently in fishes, fungi and protozoa. They exhibit a significantly conserved structure with several motifs specific to either the whole cluster or protein type. Uncoupling proteins, as well as the whole mitochondrial anion carrier gene family, probably emerged in evolution before the separation of animal, fungi, and plant kingdoms and originate from an anion/nucleotide or anion/anion transporter ancestor. Mammalian UCP1, UCP2, UCP3, and plant uncoupling proteins pUCP1 and pUCP2 are similar and seem to form one subgroup, whereas UCP4 and BMCP1 belong to a different group. Molecular, biochemical, and phylogenic data suggest that UCP2 could be considered as an UCP-prototype. UCP1 plays its biological role mainly in the non-shivering thermogenesis while the role of the other types is unknown. However, hypotheses have suggested that they are involved in the general balance of basic energy expenditure, protection from reactive oxygen species, and, in plants, in fruit ripening and seed ontogeny.

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Mitochondrial uncoupling proteins in unicellular eukaryotes

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/j.bbabio.2009.12.005 ◽

2010 ◽

Vol 1797 (6-7) ◽

pp. 792-799 ◽

Cited By ~ 37

Author(s):

Wieslawa Jarmuszkiewicz ◽

Andrzej Woyda-Ploszczyca ◽

Nina Antos-Krzeminska ◽

Francis E. Sluse

Keyword(s):

Uncoupling Proteins ◽

Mitochondrial Uncoupling ◽

Unicellular Eukaryotes ◽

Mitochondrial Uncoupling Proteins

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Immunological evidence for structural homology between Drosophila melanogaster (S14), rabbit liver (S12), Saccharomyces cerevisiae (S25), Bacillus subtilis (S6), and Escherichia coli (S6) ribosomal proteins.

Molecular and Cellular Biology ◽

10.1128/mcb.4.11.2535 ◽

1984 ◽

Vol 4 (11) ◽

pp. 2535-2539 ◽

Cited By ~ 10

Author(s):

W Y Chooi ◽

E Otaka

Keyword(s):

Escherichia Coli ◽

Saccharomyces Cerevisiae ◽

Drosophila Melanogaster ◽

Bacillus Subtilis ◽

Comparative Study ◽

Ribosomal Proteins ◽

Rabbit Liver ◽

Antigenic Determinants ◽

Structural Homology ◽

Specific Antibodies

Specific antibodies directed against Drosophila melanogaster acidic ribosomal protein S14 were used in a comparative study of eucaryotic and procaryotic ribosomes by immunoblotting and enzyme-linked immunosorbent assays. Common antigenic determinants and, thus, structural homology were found between D. melanogaster, Saccharomyces cerevisiae (S25), rabbit liver (S12), Bacillus subtilis (S6), and Escherichia coli (S6) ribosomes.

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