This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wasserfallen, A. Articles by Leisinger, T. Search for Related Content PubMed PubMed Citation Articles by Wasserfallen, A. Articles by Leisinger, T.

 Previous Article  |  Next Article 

J. Bacteriol., May 1995, 2436-2441, Vol 177, No. 9
Copyright © 1995, American Society for Microbiology

Purification and structural characterization of a flavoprotein induced by iron limitation in Methanobacterium thermoautotrophicum Marburg

A Wasserfallen, K Huber and T Leisinger
Mikrobiologisches Institut, Swiss Federal Institute of Technology, Zurich.

Cells of Methanobacterium thermoautotrophicum (strain Marburg) grown under iron-limiting conditions were found to synthesize a soluble polypeptide as one of the major cell proteins. This polypeptide purified as a homotetramer (170 kDa [subunit molecular mass, 43 kDa]) had a UV-visible spectrum typical of flavoproteins and contained 0.7 mol of flavin mononucleotide per mol of monomer. Quantitative analysis by immunoblotting with polyclonal antibodies indicated that the flavoprotein, which amounts to about 0.6% of soluble cell protein under iron-sufficient conditions (> or = 50 microM Fe2+), was induced fivefold by iron limitation (< 12 microM Fe2+). The flavoprotein- encoding gene, fprA, was cloned and sequenced. Sequence analysis revealed a well-conserved archaebacterial consensus promoter upstream of fprA, a flavodoxin signature within fprA, and 28% amino acid identity with a putative flavin mononucleotide-containing protein of Rhodobacter capsulatus which is found within an operon involved in nitrogen fixation. A possible physiological function for the flavoprotein is discussed.

This article has been cited by other articles:

• Farhoud, M. H., Wessels, H. J. C. T., Steenbakkers, P. J. M., Mattijssen, S., Wevers, R. A., van Engelen, B. G., Jetten, M. S. M., Smeitink, J. A., van den Heuvel, L. P., Keltjens, J. T. (2005). Protein Complexes in the Archaeon Methanothermobacter thermautotrophicus Analyzed by Blue Native/SDS-PAGE and Mass Spectrometry. Mol. Cell. Proteomics 4: 1653-1663 [Abstract] [Full Text]  
• Gomes, C. M., Giuffre, A., Forte, E., Vicente, J. B., Saraiva, L. M., Brunori, M., Teixeira, M. (2002). A Novel Type of Nitric-oxide Reductase. ESCHERICHIA COLI FLAVORUBREDOXIN. J. Biol. Chem. 277: 25273-25276 [Abstract] [Full Text]  
• Whiteway, J., Koziarz, P., Veall, J., Sandhu, N., Kumar, P., Hoecher, B., Lambert, I. B. (1998). Oxygen-Insensitive Nitroreductases: Analysis of the Roles of nfsA and nfsB in Development of Resistance to 5-Nitrofuran Derivatives in Escherichia coli. J. Bacteriol. 180: 5529-5539 [Abstract] [Full Text]  
• Becker, D. F., Leartsakulpanich, U., Surerus, K. K., Ferry, J. G., Ragsdale, S. W. (1998). Electrochemical and Spectroscopic Properties of the Iron-Sulfur Flavoprotein from Methanosarcina thermophila. J. Biol. Chem. 273: 26462-26469 [Abstract] [Full Text]  
• Latimer, M. T., Painter, M. H., Ferry, J. G. (1996). Characterization of an Iron-Sulfur Flavoprotein from Methanosarcina thermophila. J. Biol. Chem. 271: 24023-24028 [Abstract] [Full Text]