Uncoupling protein, H+ transport and regulation

2001 ◽  
Vol 29 (6) ◽  
pp. 806-811 ◽  
Author(s):  
M. Klingenberg ◽  
E. Winkler ◽  
K. Echtay
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Heterologous Expression ◽  
Inclusion Bodies ◽  
Uncoupling Protein ◽  
Coenzyme Q ◽  
Uncoupling Proteins ◽  
Expression In Escherichia Coli ◽  
Cl Transport

The biochemical functions of uncoupling proteins (UCPs) are discussed with the view of UCP1 as a paradigm. In contrast with UCP1, the heterologous expression of UCP3 in yeast is found to result primarily in extra-mitochondrial deposits and thus is unsuitable for studying UCP3 function. On expression in Escherichia coli inclusion bodies, UCPs extracted and incorporated into vesicles showed no H+ transport, only Cl– transport. Only after addition of coenzyme Q was fully nucleotide-sensitive high-H+ transport reconstituted, with UCP1 as well as with UCP2 and UCP3. The newly discovered cofactor role of coenzyme Q in H+ transport is proposed to imply co-operation with fatty acids for the injection of H+ into the UCP channel.

scholarly journals Characterization of a Dye-Decolorizing Peroxidase from Irpex lacteus Expressed in Escherichia coli: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates

2021 ◽  
Vol 7 (5) ◽  
pp. 325
Author(s):  
Laura Isabel de de Eugenio ◽  
Rosa Peces-Pérez ◽  
Dolores Linde ◽  
Alicia Prieto ◽  
Jorge Barriuso ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Inclusion Bodies ◽  
Veratryl Alcohol ◽  
Dye Decolorization ◽  
Irpex Lacteus ◽  
Type D ◽  
Lignin Peroxidases

A dye-decolorizing peroxidase (DyP) from Irpex lacteus was cloned and heterologously expressed as inclusion bodies in Escherichia coli. The protein was purified in one chromatographic step after its in vitro activation. It was active on ABTS, 2,6-dimethoxyphenol (DMP), and anthraquinoid and azo dyes as reported for other fungal DyPs, but it was also able to oxidize Mn2+ (as manganese peroxidases and versatile peroxidases) and veratryl alcohol (VA) (as lignin peroxidases and versatile peroxidases). This corroborated that I. lacteus DyPs are the only enzymes able to oxidize high redox potential dyes, VA and Mn+2. Phylogenetic analysis grouped this enzyme with other type D-DyPs from basidiomycetes. In addition to its interest for dye decolorization, the results of the transformation of softwood and hardwood lignosulfonates suggest a putative biological role of this enzyme in the degradation of phenolic lignin.

Mitochondrial Uncoupling Proteins in Mammals and Plants

2001 ◽  
Vol 21 (2) ◽  
pp. 201-212 ◽  
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.

scholarly journals The Role of Fatty Acids in the Activity of the Uncoupling Proteins

2009 ◽  
Vol 3 (2) ◽  
pp. 180-188 ◽  
Author(s):  
Maria d. M. Gonzalez-Barroso ◽  
Eduardo Rial
Keyword(s):  
Fatty Acids ◽  
Uncoupling Proteins

Mining Xanthomonas and Streptomyces genomes for new pectinase-encoding sequences and their heterologous expression in Escherichia coli

2008 ◽  
Vol 78 (6) ◽  
pp. 973-981 ◽  
Author(s):  
Zhizhuang Xiao ◽  
Jason Boyd ◽  
Stephan Grosse ◽  
Manon Beauchemin ◽  
Elizabeth Coupe ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Heterologous Expression ◽  
Expression In Escherichia Coli
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