Light and substrate regulation of nitrate reductase (NR) expression were compared in wild type and mutant lines of Nicotiana plumbaginifolia. Mutants affected in the NR structural gene (nia) or in the biosynthesis of the NR molybdenum cofactor (cnx) were examined. nia mutants expressing a defective apoenzyme, as well as cnx mutants, overexpressed NR mRNA, whereas nia mutants devoid of detectable NR protein had reduced or undetectable NR mRNA levels. Diurnal fluctuations of NR mRNA were specifically abolished in nia and cnx mutants, suggesting that the integrity of NR catalytic activity is required for the expression of diurnal oscillations. Unlike some fungal mutants, the nia and cnx mutants examined retained nitrate inducibility of NR expression. The possibility of autogenous control of NR expression in higher plants is discussed.
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http://dx.doi.org/10.1105/tpc.1.11.1111 | DOI Listing |
Plant Physiol Biochem
March 2023
Institute of Sciences of Food Production, C.N.R., Unit of Lecce, Lecce, Italy. Electronic address:
We report about the response of Arabidopsis thaliana to chronic and temporary Cd stress, and the Cd induced activation of ER stress and unfolded protein response (UPR). Cd-induced UPR proceeds mainly through the bZIP60 arm, which in turn activates relevant ER stress marker genes such as BiP3, CNX, PDI5 and ERdj3B in a concentration- (chronic stress) or time- (temporary stress) dependent manner. A more severe Cd-stress triggers programmed cell death (PCD) through the activation of the NAC089 transcription factor.
View Article and Find Full Text PDFPlant Physiol
March 2023
Department of Plant Molecular Biology, Biophore Building, University of Lausanne, 1015 Lausanne, Switzerland.
Accumulation of incompletely folded proteins in the endoplasmic reticulum (ER) leads to ER stress, activates ER protein degradation pathways, and upregulates genes involved in protein folding. This process is known as the unfolded protein response (UPR). The role of ER protein folding in plant responses to nutrient deficiencies is unclear.
View Article and Find Full Text PDFInt J Mol Med
August 2021
Department of Cardiology, Lihuili Hospital, Ningbo University, Ningbo, Zhejiang 315100, P.R. China.
Long QT syndrome type 2 is caused by a mutation in the human‑ether‑a‑go‑go‑related gene (HERG) gene encoding the rapidly activating delayed rectifier K‑current. HERG is a key cell membrane glycoprotein; however, whether the maturation process of HERG protein involves key molecules derived from the calnexin (CNX)/calreticulin (CRT) cycle and how these molecules work remains unknown. Using western blotting, the present study screened the key molecules CNX/CRT/endoplasmic reticulum protein 57 (ERP57) involved in this cycle, and it was revealed that the protein expression levels of CNX/CRT/ERP57 in wild‑type (WT)/A561V cells were increased compared with those in WT cells (n=3; P<0.
View Article and Find Full Text PDFEMBO J
August 2021
Faculty of Biomedical Sciences, Institute for Research in Biomedicine, Università della Svizzera italiana (USI), Bellinzona, Switzerland.
Efficient degradation of by-products of protein biogenesis maintains cellular fitness. Strikingly, the major biosynthetic compartment in eukaryotic cells, the endoplasmic reticulum (ER), lacks degradative machineries. Misfolded proteins in the ER are translocated to the cytosol for proteasomal degradation via ER-associated degradation (ERAD).
View Article and Find Full Text PDFJ Biol Chem
August 2021
Department of Biochemistry, Vanderbilt University, Nashville, Tennessee, USA; Center for Structural Biology, Vanderbilt University, Nashville, Tennessee, USA. Electronic address:
Peripheral myelin protein 22 (PMP22) folds and trafficks inefficiently, with only 20% of newly expressed protein trafficking to the cell surface. This behavior is exacerbated in many of the mutants associated with Charcot-Marie-Tooth disease, motivating further study. Here we characterized the role of N-glycosylation in limiting PMP22 trafficking.
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