Identification of three urease accessory proteins that are required for urease activation in Arabidopsis
Witte C-P, Rosso MG, Romeis T (2005)
Plant Physiology 139(3): 1155-1162.
Zeitschriftenaufsatz
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Autor*in
Witte, Claus-Peter;
Rosso, Mario G.;
Romeis, Tina
Einrichtung
Abstract / Bemerkung
Urease is a nickel-containing urea hydrolase involved in nitrogen recycling from ureide, purine, and arginine catabolism in plants. The process of urease activation by incorporation of nickel into the active site is a prime example of chaperone-mediated metal transfer to an enzyme. Four urease accessory proteins are required for activation in Klebsiella aerogenes. In plants urease accessory proteins have so far been only partially defined. Using reverse genetic tools we identified four genes that are necessary for urease activity in Arabidopsis (Arabidopsis thaliana; ecotypes Columbia and Nössen). Plants bearing T-DNA or Ds element insertions in either the structural gene for urease or in any of the three putative urease accessory genes AtureD, AtureF, and AtureG lacked the corresponding mRNAs and were defective in urease activity. In contrast to wild-type plants, the mutant lines were not able to support growth with urea as the sole nitrogen source. To investigate whether the identified accessory proteins would be sufficient to support eukaryotic urease activation, the corresponding cDNAs were introduced into urease-negative Escherichia coli. In these bacteria, urease activity was observed only when all three plant accessory genes were coexpressed together with the plant urease gene. Remarkably, plant urease activation occurred as well in cell-free E. coli extracts, but only in extracts from cells that had expressed all three accessory proteins. The future molecular dissection of the plant urease activation process may therefore be performed in vitro, providing a powerful tool to further our understanding of the biochemistry of chaperone-mediated metal transfer processes in plants.
Stichworte
Nitrates;
Mutation;
Quaternary Ammonium Compounds;
Reverse Transcriptase Polymerase Chain Reaction;
Enzyme Activation;
Escherichia coli;
Molecular Sequence Data;
RNA;
Arabidopsis Proteins;
Arabidopsis;
Messenger;
Urease;
Urea
Erscheinungsjahr
2005
Zeitschriftentitel
Plant Physiology
Band
139
Ausgabe
3
Seite(n)
1155-1162
ISSN
0032-0889
eISSN
1532-2548
Page URI
https://pub.uni-bielefeld.de/record/1996259
Zitieren
Witte C-P, Rosso MG, Romeis T. Identification of three urease accessory proteins that are required for urease activation in Arabidopsis. Plant Physiology. 2005;139(3):1155-1162.
Witte, C. - P., Rosso, M. G., & Romeis, T. (2005). Identification of three urease accessory proteins that are required for urease activation in Arabidopsis. Plant Physiology, 139(3), 1155-1162. https://doi.org/10.1104/pp.105.070292
Witte, Claus-Peter, Rosso, Mario G., and Romeis, Tina. 2005. “Identification of three urease accessory proteins that are required for urease activation in Arabidopsis”. Plant Physiology 139 (3): 1155-1162.
Witte, C. - P., Rosso, M. G., and Romeis, T. (2005). Identification of three urease accessory proteins that are required for urease activation in Arabidopsis. Plant Physiology 139, 1155-1162.
Witte, C.-P., Rosso, M.G., & Romeis, T., 2005. Identification of three urease accessory proteins that are required for urease activation in Arabidopsis. Plant Physiology, 139(3), p 1155-1162.
C.-P. Witte, M.G. Rosso, and T. Romeis, “Identification of three urease accessory proteins that are required for urease activation in Arabidopsis”, Plant Physiology, vol. 139, 2005, pp. 1155-1162.
Witte, C.-P., Rosso, M.G., Romeis, T.: Identification of three urease accessory proteins that are required for urease activation in Arabidopsis. Plant Physiology. 139, 1155-1162 (2005).
Witte, Claus-Peter, Rosso, Mario G., and Romeis, Tina. “Identification of three urease accessory proteins that are required for urease activation in Arabidopsis”. Plant Physiology 139.3 (2005): 1155-1162.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
UNIPROT
8 Einträge gefunden, die diesen Artikel zitieren
Urease accessory protein G (UNIPROT: F4IHW4)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
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Urease accessory protein D (UNIPROT: F4IIY7)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
Urease accessory protein G (UNIPROT: O64700)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
Urease accessory protein D (UNIPROT: F4IIY7)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
Urease accessory protein G (UNIPROT: F4IHW4)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
Urease accessory protein D (UNIPROT: Q7Y0S0)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
Urease accessory protein F (UNIPROT: Q9XHZ3)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
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Functional characterisation of urease accessory protein G (ureG) from potato.
Witte CP, Isidore E, Tiller SA, Davies HV, Taylor MA., Plant Mol. Biol. 45(2), 2001
PMID: 11289508
Witte CP, Isidore E, Tiller SA, Davies HV, Taylor MA., Plant Mol. Biol. 45(2), 2001
PMID: 11289508
Subcellular localization and oligomerization of the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 protein.
Shah K, Gadella TW Jr, van Erp H, Hecht V, de Vries SC., J. Mol. Biol. 309(3), 2001
PMID: 11397085
Shah K, Gadella TW Jr, van Erp H, Hecht V, de Vries SC., J. Mol. Biol. 309(3), 2001
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Leaf urea metabolism in potato. Urease activity profile and patterns of recovery and distribution of (15)N after foliar urea application in wild-type and urease-antisense transgenics.
Witte CP, Tiller SA, Taylor MA, Davies HV., Plant Physiol. 128(3), 2002
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Witte CP, Tiller SA, Taylor MA, Davies HV., Plant Physiol. 128(3), 2002
PMID: 11891267
Activation of the urease of Schizosaccharomyces pombe by the UreF accessory protein from soybean.
Bacanamwo M, Witte CP, Lubbers MW, Polacco JC., Mol. Genet. Genomics 268(4), 2002
PMID: 12471450
Bacanamwo M, Witte CP, Lubbers MW, Polacco JC., Mol. Genet. Genomics 268(4), 2002
PMID: 12471450
Nickel uptake and utilization by microorganisms.
Mulrooney SB, Hausinger RP., FEMS Microbiol. Rev. 27(2-3), 2003
PMID: 12829270
Mulrooney SB, Hausinger RP., FEMS Microbiol. Rev. 27(2-3), 2003
PMID: 12829270
Stable isotope labeling of phosphopeptides for multiparallel kinase target analysis and identification of phosphorylation sites.
Glinski M, Romeis T, Witte CP, Wienkoop S, Weckwerth W., Rapid Commun. Mass Spectrom. 17(14), 2003
PMID: 12845583
Glinski M, Romeis T, Witte CP, Wienkoop S, Weckwerth W., Rapid Commun. Mass Spectrom. 17(14), 2003
PMID: 12845583
Genome-wide insertional mutagenesis of Arabidopsis thaliana.
Alonso JM, Stepanova AN, Leisse TJ, Kim CJ, Chen H, Shinn P, Stevenson DK, Zimmerman J, Barajas P, Cheuk R, Gadrinab C, Heller C, Jeske A, Koesema E, Meyers CC, Parker H, Prednis L, Ansari Y, Choy N, Deen H, Geralt M, Hazari N, Hom E, Karnes M, Mulholland C, Ndubaku R, Schmidt I, Guzman P, Aguilar-Henonin L, Schmid M, Weigel D, Carter DE, Marchand T, Risseeuw E, Brogden D, Zeko A, Crosby WL, Berry CC, Ecker JR., Science 301(5633), 2003
PMID: 12893945
Alonso JM, Stepanova AN, Leisse TJ, Kim CJ, Chen H, Shinn P, Stevenson DK, Zimmerman J, Barajas P, Cheuk R, Gadrinab C, Heller C, Jeske A, Koesema E, Meyers CC, Parker H, Prednis L, Ansari Y, Choy N, Deen H, Geralt M, Hazari N, Hom E, Karnes M, Mulholland C, Ndubaku R, Schmidt I, Guzman P, Aguilar-Henonin L, Schmid M, Weigel D, Carter DE, Marchand T, Risseeuw E, Brogden D, Zeko A, Crosby WL, Berry CC, Ecker JR., Science 301(5633), 2003
PMID: 12893945
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