Novel thioredoxin targets in Dictyostelium discoideum identified by two-hybrid analysis: interactions of thioredoxin with elongation factor 1α and yeast alcohol dehydrogenase

Verfasser / Beitragende:
[Thomas Brodegger, Anja Stockmann, Jürgen Oberstraß, Wolfgang Nellen, Hartmut Follmann]
Ort, Verlag, Jahr:
2004
Enthalten in:
Biological Chemistry, 385/12(2004-12-01), 1185-1192
Format:
Artikel (online)
ID: 378896040
LEADER caa a22 4500
001 378896040
003 CHVBK
005 20180305123506.0
007 cr unu---uuuuu
008 161128e20041201xx s 000 0 eng
024 7 0 |a 10.1515/BC.2004.153  |2 doi 
035 |a (NATIONALLICENCE)gruyter-10.1515/BC.2004.153 
245 0 0 |a Novel thioredoxin targets in Dictyostelium discoideum identified by two-hybrid analysis: interactions of thioredoxin with elongation factor 1α and yeast alcohol dehydrogenase  |h [Elektronische Daten]  |c [Thomas Brodegger, Anja Stockmann, Jürgen Oberstraß, Wolfgang Nellen, Hartmut Follmann] 
520 3 |a Thioredoxins (Trx) are ubiquitous dicysteine proteins capable of modulating enzymes and other cellular targets through specific disulfide-dithiol redox changes. They are unique in that a large number of very diverse metabolic systems are addressed and redox-regulated in bacteria, animal, and plant cells, but the finite number of thioredoxin interaction partners is still unknown. Two-hybrid methodology should provide a rational way to establish thioredoxin functions in a given organism. We report a search for physiological target proteins of thioredoxin1 in the social amoeba Dictyostelium discoideum, which possesses three developmentally regulated thioredoxin genes, all of which lack functional characterisation. A two-hybrid approach identified at least seven bona fide thioredoxin partners, including oxidoreductases, proteins of the ribosomal translation apparatus, and the cytoskeletal protein filopodin. With the exception of ribonucleotide reductase, none of these systems had previously been linked to specific redox modulation. Molecular interactions in two of the new thioredoxin/target protein couples were verified by biochemical studies: (1) thioredoxin1 and the abundant elongation factor 1α from D. discoideum form the mixed heterodisulfide characteristic of the thioredoxin mechanism of action; and (2) reduced thioredoxin, but not glutathione, strongly inhibits yeast alcohol dehydrogenase catalysis of ethanol oxidation. 
540 |a ©2004 by Walter de Gruyter Berlin New York 
690 7 |a Biochemistry  |2 nationallicence 
690 7 |a Molecular biology  |2 nationallicence 
690 7 |a Cellular biology  |2 nationallicence 
690 7 |a alcohol dehydrogenase  |2 nationallicence 
690 7 |a disulfide formation  |2 nationallicence 
690 7 |a elongation factors  |2 nationallicence 
690 7 |a enzyme regulation  |2 nationallicence 
690 7 |a thioredoxins  |2 nationallicence 
690 7 |a thioredoxin oligomers  |2 nationallicence 
700 1 |a Brodegger  |D Thomas  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
700 1 |a Stockmann  |D Anja  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
700 1 |a Oberstraß  |D Jürgen  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
700 1 |a Nellen  |D Wolfgang  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
700 1 |a Follmann  |D Hartmut  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
773 0 |t Biological Chemistry  |d Walter de Gruyter  |g 385/12(2004-12-01), 1185-1192  |x 1431-6730  |q 385:12<1185  |1 2004  |2 385  |o bchm 
856 4 0 |u https://doi.org/10.1515/BC.2004.153  |q text/html  |z Onlinezugriff via DOI 
908 |D 1  |a research article  |2 jats 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1515/BC.2004.153  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Brodegger  |D Thomas  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Stockmann  |D Anja  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Oberstraß  |D Jürgen  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Nellen  |D Wolfgang  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Follmann  |D Hartmut  |u Departments of Biochemistry and Genetics, Natural Sciences Faculty, University of Kassel, D-34109 Kassel, Germany  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Biological Chemistry  |d Walter de Gruyter  |g 385/12(2004-12-01), 1185-1192  |x 1431-6730  |q 385:12<1185  |1 2004  |2 385  |o bchm 
900 7 |b CC0  |u http://creativecommons.org/publicdomain/zero/1.0  |2 nationallicence 
898 |a BK010053  |b XK010053  |c XK010000 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-gruyter