Fur (ferric uptake regulator) is a prokaryotic transcriptional regulator that controls a large number of genes mainly related to iron metabolism. Several Fur homologues with different physiological roles are frequently found in the same organism. The genome of the filamentous cyanobacterium Anabaena (Nostoc) sp. PCC 7120 codes for three different fur genes. FurA is an essential protein involved in iron homoeostasis that also modulates dinitrogen fixation. FurA interacts with haem, impairing its DNA-binding ability. To explore functional differences between Fur homologues in Anabaena, factors affecting their regulation, as well as some biochemical characteristics, have been investigated. Although incubation of FurB with haem severely hinders its ability to interact with DNA, binding of haem to FurC could not be detected. Oxidative stress enhances the transcription of the three fur genes, especially that of furB and furC. In addition, overexpression of FurA and FurB in Escherichia coli increases survival when the cells are challenged with H2O2 or Methyl Viologen (paraquat), a superoxide-anion-generating reagent. When present in saturating concentrations, FurB exhibits unspecific DNA-binding activity and protects DNA from cleavage produced by hydroxyl radicals or DNaseI. On the basis of these results, we suggest that, whereas at low concentrations FurB would act as a member of the Fur family, at saturating concentrations FurB protects DNA, showing a DNA-protection-during-starvation-like behaviour.
Skip Nav Destination
Article navigation
February 2009
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkEditorial Board
Research Article|
January 28 2009
New insights into the role of Fur proteins: FurB (All2473) from Anabaena protects DNA and increases cell survival under oxidative stress
Sara López-Gomollón;
Sara López-Gomollón
*Department of Biochemistry and Molecular and Cell Biology, University of Zaragoza, Pedro Cerbuna 12, 50009 Zaragoza, Spain
†BiFi (Biocomputation and Complex Systems Physics Institute), University of Zaragoza, Corona de Aragón 42, 50009 Zaragoza, Spain
Search for other works by this author on:
Emma Sevilla;
Emma Sevilla
*Department of Biochemistry and Molecular and Cell Biology, University of Zaragoza, Pedro Cerbuna 12, 50009 Zaragoza, Spain
†BiFi (Biocomputation and Complex Systems Physics Institute), University of Zaragoza, Corona de Aragón 42, 50009 Zaragoza, Spain
Search for other works by this author on:
M. Teresa Bes;
M. Teresa Bes
*Department of Biochemistry and Molecular and Cell Biology, University of Zaragoza, Pedro Cerbuna 12, 50009 Zaragoza, Spain
†BiFi (Biocomputation and Complex Systems Physics Institute), University of Zaragoza, Corona de Aragón 42, 50009 Zaragoza, Spain
Search for other works by this author on:
M. Luisa Peleato;
M. Luisa Peleato
*Department of Biochemistry and Molecular and Cell Biology, University of Zaragoza, Pedro Cerbuna 12, 50009 Zaragoza, Spain
†BiFi (Biocomputation and Complex Systems Physics Institute), University of Zaragoza, Corona de Aragón 42, 50009 Zaragoza, Spain
Search for other works by this author on:
María F. Fillat
María F. Fillat
1
*Department of Biochemistry and Molecular and Cell Biology, University of Zaragoza, Pedro Cerbuna 12, 50009 Zaragoza, Spain
†BiFi (Biocomputation and Complex Systems Physics Institute), University of Zaragoza, Corona de Aragón 42, 50009 Zaragoza, Spain
1To whom correspondence should be addressed (email fillat@unizar.es).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
July 04 2008
Revision Received:
October 21 2008
Accepted:
October 22 2008
Accepted Manuscript online:
October 22 2008
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem J (2009) 418 (1): 201–207.
Article history
Received:
July 04 2008
Revision Received:
October 21 2008
Accepted:
October 22 2008
Accepted Manuscript online:
October 22 2008
Citation
Sara López-Gomollón, Emma Sevilla, M. Teresa Bes, M. Luisa Peleato, María F. Fillat; New insights into the role of Fur proteins: FurB (All2473) from Anabaena protects DNA and increases cell survival under oxidative stress. Biochem J 15 February 2009; 418 (1): 201–207. doi: https://doi.org/10.1042/BJ20081066
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Captcha Validation Error. Please try again.