High affinity binding of albicidin phytotoxins by the AlbA protein from Klebsiella oxytoca

Zhang, LH, Xu, JL and Birch, RG (1998) High affinity binding of albicidin phytotoxins by the AlbA protein from Klebsiella oxytoca. Microbiology-uk, 144 2: 555-559.

Author Zhang, LH
Xu, JL
Birch, RG
Title High affinity binding of albicidin phytotoxins by the AlbA protein from Klebsiella oxytoca
Journal name Microbiology-uk   Check publisher's open access policy
ISSN 1350-0872
Publication date 1998-01-01
Sub-type Article (original research)
Volume 144
Issue 2
Start page 555
End page 559
Total pages 5
Language eng
Abstract Albicidins are a family of phytotoxins and antibiotics which play an important role in the pathogenesis of sugarcane leaf scald disease. The albA gene from Klebsiella oxytoca encodes a protein which inactivates albicidin by heat-reversible binding. Albicidin ligand binding to a recombinant AlbA protein, purified by means of a glutathione S-transferase gene fusion system, is an almost instant and saturable reaction. Kinetic and stoichiometric analysis of the binding reaction indicated the presence of a single high affinity binding site with a dissociation constant of 6.4 x 10(-8) M. The AlbA-albicidin complex is stable from 4 to 40 degrees C, from ph 5 to 9 and in high salt solutions. Treatment with protein denaturants released all bound albicidin. These properties indicate that AlbA may be a useful affinity matrix for selective purification of albicidin antibiotics. AlbA does not bind to p-nitrophenyl butyrate or alpha-naphthyl butyrate, the substrates of the albicidin detoxification enzyme AlbD from Pantoea dispersa. The potential exists to pyramid genes for different mechanisms in transgenic plants to protect plastid DNA replication from inhibition by albicidins.
Keyword Microbiology
Albicidin Inactivation
Albicidin Binding Protein
Phytotoxin And Disease Resistance
Affinity Matrix
Binding Kinetics
Escherichia-coli
Xanthomonas-albilineans
Resistance
Sugarcane
Chlorosis
Gene
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Biological Sciences Publications
 
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Created: Mon, 13 Aug 2007, 20:20:45 EST