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 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

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

scholarly journals Colonization of Arabidopsis thaliana with Salmonella enterica and Enterohemorrhagic Escherichia coli O157:H7 and Competition by Enterobacter asburiae

2003 ◽  
Vol 69 (8) ◽  
pp. 4915-4926 ◽  
Author(s):  
Michael B. Cooley ◽  
William G. Miller ◽  
Robert E. Mandrell
Keyword(s):  
Escherichia Coli ◽  
Arabidopsis Thaliana ◽  
Salmonella Enterica ◽  
Fluorescent Protein ◽  
Enterohemorrhagic Escherichia Coli ◽  
Plant Responses ◽  
Human Pathogens ◽  
E Coli ◽  
Green Fluorescent ◽  
Enterobacter Asburiae

ABSTRACT Enteric pathogens, such as Salmonella enterica and Escherichia coli O157:H7, have been shown to contaminate fresh produce. Under appropriate conditions, these bacteria will grow on and invade the plant tissue. We have developed Arabidopsis thaliana (thale cress) as a model system with the intention of studying plant responses to human pathogens. Under sterile conditions and at 100% humidity, S. enterica serovar Newport and E. coli O157:H7 grew to 109 CFU g−1 on A. thaliana roots and to 2 × 107 CFU g−1 on shoots. Furthermore, root inoculation led to contamination of the entire plant, indicating that the pathogens are capable of moving on or within the plant in the absence of competition. Inoculation with green fluorescent protein-labeled S. enterica and E. coli O157:H7 showed invasion of the roots at lateral root junctions. Movement was eliminated and invasion decreased when nonmotile mutants of S. enterica were used. Survival of S. enterica serovar Newport and E. coli O157:H7 on soil-grown plants declined as the plants matured, but both pathogens were detectable for at least 21 days. Survival of the pathogen was reduced in unautoclaved soil and amended soil, suggesting competition from indigenous epiphytes from the soil. Enterobacter asburiae was isolated from soil-grown A. thaliana and shown to be effective at suppressing epiphytic growth of both pathogens under gnotobiotic conditions. Seed and chaff harvested from contaminated plants were occasionally contaminated. The rate of recovery of S. enterica and E. coli O157:H7 from seed varied from undetectable to 19% of the seed pools tested, depending on the method of inoculation. Seed contamination by these pathogens was undetectable in the presence of the competitor, Enterobacter asburiae. Sampling of 74 pools of chaff indicated a strong correlation between contamination of the chaff and seed (P = 0.025). This suggested that contamination of the seed occurred directly from contaminated chaff or by invasion of the flower or silique. However, contaminated seeds were not sanitized by extensive washing and chlorine treatment, indicating that some of the bacteria reside in a protected niche on the seed surface or under the seed coat.

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

1988 ◽  
Vol 8 (1) ◽  
pp. 371-380
Author(s):  
T W McMullin ◽  
R L Hallberg
Keyword(s):  
Escherichia Coli ◽  
Tetrahymena Thermophila ◽  
Mitochondrial Protein ◽  
Cross Reactivity ◽  
Macromolecular Complexes ◽  
E Coli ◽  
Groel Gene ◽  
Evolutionarily Conserved ◽  
Associated Proteins ◽  
Related Proteins

We recently reported that a Tetrahymena thermophila 58-kilodalton (kDa) mitochondrial protein (hsp58) was selectively synthesized during heat shock. In this study, we show that hsp58 displayed antigenic similarity with mitochondrially associated proteins from Saccharomyces cerevisiae (64 kDa), Xenopus laevis (60 kDa), Zea mays (62 kDa), and human cells (59 kDa). Furthermore, a 58-kDa protein from Escherichia coli also exhibited antigenic cross-reactivity to an antiserum directed against the T. thermophila mitochondrial protein. The proteins from S. cerevisiae and E. coli antigenically related to hsp58 were studied in detail and found to share several other characteristics with hsp58, including heat inducibility and the property of associating into distinct oligomeric complexes. The T. thermophila, S. cerevisiae, and E. coli macromolecular complexes containing these related proteins had similar sedimentation characteristics and virtually identical morphologies as seen with the electron microscope. The distinctive properties of the E. coli homolog to T. thermophila hsp58 indicate that it is most likely the product of the groEL gene.

A 13-kilodalton maize mitochondrial protein in E. coli confers sensitivity to Bipolaris maydis toxin

Science ◽  
1988 ◽  
Vol 239 (4837) ◽  
pp. 293-295 ◽  
Author(s):  
R. Dewey ◽  
J. Siedow ◽  
D. Timothy ◽  
C. Levings
Keyword(s):  
Mitochondrial Protein ◽  
Bipolaris Maydis ◽  
E Coli

Construction of Two Vectors for a Bypass of Monocotyledon Plants Photorespiration

2011 ◽  
Vol 340 ◽  
pp. 351-356
Author(s):  
Xue Liang Bai ◽  
Dan Wang ◽  
Ning Ning Liu ◽  
Li Jing Wei ◽  
Ye Rong Zhu ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Transgenic Plants ◽  
Binary Vector ◽  
Transit Peptide ◽  
Expression Vectors ◽  
Chloroplast Transit Peptide ◽  
E Coli ◽  
Plant Expression ◽  
Glycolate Dehydrogenase ◽  
Save Energy

In order to modify the photorespiration of monocotyledonous crops, we aimed to construct vectors that will be used to introduce a bypass to the native photorespiration pathway. Firstly, we cloned the encoding sequences of glyoxylate carboligase (GCL) and tartronic semialdehyde reductase (TSR) fromE. coli, glycolate dehydrogenase (GDH) fromArabidopsis thalianaand chloroplast transit peptide (cTP) from rice. Then we constructed a universal vector pEXP harboring the encoding sequence of cTP for targeting a protein into chloroplast. By insertion of these three encoding sequences into the universal vector pEXP, we obtained the expression cassettes for GCL, TSR and GDH, respectively. Finally, we inserted the cassettes for GCL and TSR in tandem into the binary vector pCAMBIA 1301, and for GDH into another binary vector, pPGN, to obtain our plant expression vectors pCAMBIA 1301-TG and pPGN-GDH, respectively. These two expression vectors possess different selection resistance and can be used to transform monocots together, to introduce the bypass pathway of photorespiration. By this way, the transgenic plants can recycle glycolate, the by-product of photosynthesis in C3plants, within the chloroplast, simultaneously, save energy and avoid the loss of ammonia, which will contribute to improved growth.

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