High-throughput analysis reveals disturbances throughout the cell caused by Arabidopsis UCP1 and UCP3 double knockdown.

Three genes encoding mitochondrial uncoupling proteins (UCPs) have been described in Arabidopsis thaliana (UCP1 to UCP3). In plants, UCPs may act as an uncoupler or as an aspartate/glutamate exchanger. For instance, much of the data regarding UCP functionality were obtained for the UCP1 and UCP2 isoforms compared with UCP3.

Metabolism and Signaling of Plant Mitochondria in Adaptation to Environmental Stresses.

The interaction of mitochondria with cellular components evolved differently in plants and mammals; in plants, the organelle contains proteins such as ALTERNATIVE OXIDASES (AOXs), which, in conjunction with internal and external ALTERNATIVE NAD(P)H DEHYDROGENASES, allow canonical oxidative phosphorylation (OXPHOS) to be bypassed. Plant mitochondria also contain UNCOUPLING PROTEINS (UCPs) that bypass OXPHOS. Recent work revealed that OXPHOS bypass performed by AOXs and UCPs is linked with new mechanisms of mitochondrial retrograde signaling.

The double knockdown of the mitochondrial uncoupling protein isoforms reveals partial redundant roles during Arabidopsis thaliana vegetative and reproductive development.

Mitochondrial uncoupling proteins (UCPs) are specialized proteins capable of dissipating the proton electrochemical gradient generated in respiration independent of ATP synthesis. Three UCP coding genes with distinct expression patterns have been identified in Arabidopsis thaliana (namely UCP1, UCP2 and UCP3). Here, we generated T-DNA double-insertion mutants (ucp1 ucp2, ucp1 ucp3 and ucp2 ucp3) to investigate the functionality of the Arabidopsis UCP isoforms.

Glufosinate Resistance Level is Proportional to Phosphinothricin Acetyltransferase Gene Expression in Glufosinate-Resistant Maize.

Phosphinothricin acetyltransferase ( pat) gene confers resistance to glufosinate by transforming this herbicide into N-acetyl-l-glufosinate (NAG). The pat gene was inserted in six maize hybrids (Herculex, Agrisure TL, Herculex Yieldgard, Leptra, Viptera 3, Power Core) as a selectable marker, and its expression was evaluated by qPCR in comparison with the maize glufosinate-susceptible cultivar VTPRO. In addition, the levels of NAG, glufosinate degradation, ammonia accumulation, electron transport rate (ETR), visual injury, and biomass were also investigated.

Overexpression of UCP1 in tobacco induces mitochondrial biogenesis and amplifies a broad stress response.

Background: Uncoupling protein one (UCP1) is a mitochondrial inner membrane protein capable of uncoupling the electrochemical gradient from adenosine-5'-triphosphate (ATP) synthesis, dissipating energy as heat. UCP1 plays a central role in nonshivering thermogenesis in the brown adipose tissue (BAT) of hibernating animals and small rodents. A UCP1 ortholog also occurs in plants, and aside from its role in uncoupling respiration from ATP synthesis, thereby wasting energy, it plays a beneficial role in the plant response to several abiotic stresses, possibly by decreasing the production of reactive oxygen species (ROS) and regulating cellular redox homeostasis.

The 20S proteasome α5 subunit of Arabidopsis thaliana carries an RNase activity and interacts in planta with the lettuce mosaic potyvirus HcPro protein.

In plants, the ubiquitin/26S proteasome system (UPS) plays a central role in protein degradation and is involved in many steps of defence mechanisms, regardless of the types of pathogen targeted. In addition to its proteolytic activities, the UPS ribonuclease (RNase) activity, previously detected in 20S proteasome preparations from cauliflower and sunflower (Helianthus annuus), has been shown to specifically target plant viral RNAs in vitro. In this study, we show that recombinant Arabidopsis thaliana proteasomal α(5) subunit expressed in Escherichia coli harbours an RNase activity that degrades Tobacco mosaic virus (TMV, Tobamovirus)- and Lettuce mosaic virus (LMV, Potyvirus)-derived RNAs in vitro.

Plant uncoupling mitochondrial proteins.

Uncoupling proteins (UCPs) are membrane proteins that mediate purine nucleotide-sensitive free fatty acid-activated H(+) flux through the inner mitochondrial membrane. After the discovery of UCP in higher plants in 1995, it was acknowledged that these proteins are widely distributed in eukaryotic organisms. The widespread presence of UCPs in eukaryotes implies that these proteins may have functions other than thermogenesis.