scholarly journals Mutational analysis of Arabidopsis thaliana plant uncoupling mitochondrial protein

2007 ◽  
Vol 1767 (12) ◽  
pp. 1412-1417 ◽  
Author(s):  
Regiane Degan Fávaro ◽  
Jiri Borecký ◽  
Débora Colombi ◽  
Aníbal E. Vercesi ◽  
Ivan G. Maia
Keyword(s):  
Arabidopsis Thaliana ◽  
Mutational Analysis ◽  
Mitochondrial Protein ◽  
Plant Uncoupling Mitochondrial Protein

Functional reconstitution of Arabidopsis thaliana plant uncoupling mitochondrial protein (PUMP) expressed in E. coli

2000 ◽  
Vol 28 (5) ◽  
pp. A187-A187
Author(s):  
Jiri Borecky ◽  
Ivan G. Maia ◽  
Alexandre D. T. Costa ◽  
Paula Bresciani Martins de Andrade ◽  
Petr Jezek ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Mitochondrial Protein ◽  
E Coli ◽  
Plant Uncoupling Mitochondrial Protein

Functional reconstitution of Arabidopsis thaliana plant uncoupling mitochondrial protein (At PUMP1) expressed in Escherichia coli

FEBS Letters ◽  
2001 ◽  
Vol 505 (2) ◽  
pp. 240-244 ◽  
Author(s):  
Jirı́ Borecký ◽  
Ivan G. Maia ◽  
Alexandre D.T. Costa ◽  
Petr Ježek ◽  
Hernan Chaimovich ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Arabidopsis Thaliana ◽  
Mitochondrial Protein ◽  
Plant Uncoupling Mitochondrial Protein

scholarly journals Linoleic Acid-induced Activity of Plant Uncoupling Mitochondrial Protein in Purified Tomato Fruit Mitochondria during Resting, Phosphorylating, and Progressively Uncoupled Respiration

1998 ◽  
Vol 273 (52) ◽  
pp. 34882-34886 ◽  
Author(s):  
Wieslawa Jarmuszkiewicz ◽  
Andrea Miyasaka Almeida ◽  
Claudine M. Sluse-Goffart ◽  
Francis E. Sluse ◽  
Anibal E. Vercesi
Keyword(s):  
Linoleic Acid ◽  
Tomato Fruit ◽  
Mitochondrial Protein ◽  
Plant Uncoupling Mitochondrial Protein

scholarly journals Evidence for Anion-translocating Plant Uncoupling Mitochondrial Protein in Potato Mitochondria

1996 ◽  
Vol 271 (51) ◽  
pp. 32743-32748 ◽  
Author(s):  
Petr Ježek ◽  
Alexandre D. T. Costa ◽  
Anibal E. Vercesi
Keyword(s):  
Mitochondrial Protein ◽  
Plant Uncoupling Mitochondrial Protein

Root Morphology Mutants in Arabidopsis thaliana

1992 ◽  
Vol 19 (4) ◽  
pp. 427 ◽  
Author(s):  
TI Baskin ◽  
AS Betzner ◽  
R Hoggart ◽  
A Cork ◽  
RE Williamson
Keyword(s):  
Arabidopsis Thaliana ◽  
Root Growth ◽  
Mutational Analysis ◽  
Root Apex ◽  
Temperature Sensitive ◽  
Restrictive Temperature ◽  
Wild Type ◽  
In The Wild ◽  
Root Morphogenesis ◽  
Type Rate

We have begun a mutational analysis of root morphogenesis in Arabidopsis thaliana. We report here the initial genetic and physiological characterisation of six mutations that affect root growth and development. Three of them (rsw1, rsw2, rsw3) cause extensive radial swelling of the root apex. These mutations are recessive at different loci and show temperature-sensitive expression, such that the roots appear wild type when grown at 18�C but express the mutant phenotype when transferred to 31�C. Following transfer to the restrictive temperature, these three mutations have different kinetic and morphological patterns of radial swelling, and grow at different rates with continued time at high temperature. We believe that these mutations represent three different loci active in the wild type in regulating the shape of the root. We have also characterised two mutations that affect only the root epidermis, causing many epidermal cells to bulge (reb1-1, reb1-2). The two mutations are recessive and are alleles. However, rebl-1 is constitutive whereas reb1-2 is temperature sensitive, only expressing at 33�C. Reb1-2 also causes a deviation from the normal straight growth of the root such that the affected roots grow with sharp bends or meanders. The final mutant reported here is a stunted plant (stp1), in which the root growth rate is approximately 25% of the wild type rate. Moreover, root growth steadily accelerates over 5 days following germination in the wild type but remains constant in stp1, which grows at a constant rate over the same interval.

scholarly journals Mutational analysis of the AtNUDT7 Nudix hydrolase from Arabidopsis thaliana reveals residues required for protein quaternary structure formation and activity.

2009 ◽  
Vol 56 (2) ◽  
Author(s):  
Kamil Olejnik ◽  
Danuta Płochocka ◽  
Marcin Grynberg ◽  
Grazyna Goch ◽  
Wiesław I Gruszecki ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Quaternary Structure ◽  
Mutational Analysis ◽  
Negative Control ◽  
Attenuated Total Reflection ◽  
Site Directed Mutagenesis ◽  
Regulatory Function ◽  
Nudix Hydrolase ◽  
Mutant Proteins ◽  
Signaling Complex

Arabidopsis thaliana AtNUDT7, a homodimeric Nudix hydrolase active on ADP-ribose and NADH, exerts negative control on the major signaling complex involved in plant defense activation and programmed cell death. The structural and functional consequences of altering several amino-acid residues of the AtNUDT7 protein have been examined by site-directed mutagenesis, far-UV circular dichroism (CD), attenuated total reflection-Fourier transform infrared (ATR-FTIR) and photon correlation (PCS) spectroscopy, biochemical analysis and protein-protein interaction studies. Alanine substitutions of F73 and V168 disallowed dimer formation. Both the F73A- and V168A-mutated proteins displayed no observable enzymatic activity. Alanine substitution of the V69 residue did not significantly alter the enzyme activity and had no influence on dimer arrangement. The non-conserved V26 residue, used as a negative control, did not contribute to the enzyme quaternary structure or activity. Detailed biophysical characterization of the wild-type and mutant proteins indicates that the mutations do not considerably alter the secondary structure of the enzyme but they affect dimer assembly. In addition, mutating residues V69, F73 and V168 disrupted the binding of AtNUDT7 to the regulatory 14.3.3 protein. These are the first studies of the structure-function relationship of AtNUDT7, a Nudix hydrolase of important regulatory function.

scholarly journals Intronic tRNAs of mitochondrial origin regulate constitutive and alternative splicing

2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Simon M. Hoser ◽  
Anne Hoffmann ◽  
Andreas Meindl ◽  
Maximilian Gamper ◽  
Jörg Fallmann ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Human Genome ◽  
Splice Site ◽  
Mutational Analysis ◽  
Mitochondrial Protein ◽  
Regulatory Elements ◽  
Trna Genes ◽  
Mitochondrial Trna ◽  
Mobility Shift ◽  
Cloverleaf Structure

Abstract Background The presence of nuclear mitochondrial DNA (numtDNA) has been reported within several nuclear genomes. Next to mitochondrial protein-coding genes, numtDNA sequences also encode for mitochondrial tRNA genes. However, the biological roles of numtDNA remain elusive. Results Employing in silico analysis, we identify 281 mitochondrial tRNA homologs in the human genome, which we term nimtRNAs (nuclear intronic mitochondrial-derived tRNAs), being contained within introns of 76 nuclear host genes. Despite base changes in nimtRNAs when compared to their mtRNA homologs, a canonical tRNA cloverleaf structure is maintained. To address potential functions of intronic nimtRNAs, we insert them into introns of constitutive and alternative splicing reporters and demonstrate that nimtRNAs promote pre-mRNA splicing, dependent on the number and positioning of nimtRNA genes and splice site recognition efficiency. A mutational analysis reveals that the nimtRNA cloverleaf structure is required for the observed splicing increase. Utilizing a CRISPR/Cas9 approach, we show that a partial deletion of a single endogenous nimtRNALys within intron 28 of the PPFIBP1 gene decreases inclusion of the downstream-located exon 29 of the PPFIBP1 mRNA. By employing a pull-down approach followed by mass spectrometry, a 3′-splice site-associated protein network is identified, including KHDRBS1, which we show directly interacts with nimtRNATyr by an electrophoretic mobility shift assay. Conclusions We propose that nimtRNAs, along with associated protein factors, can act as a novel class of intronic splicing regulatory elements in the human genome by participating in the regulation of splicing.

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