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

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, February 2002, p. 745-755, Vol. 68, No. 2
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.2.745-755.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Molecular Analyses of the Natural Transformation Machinery and Identification of Pilus Structures in the Extremely Thermophilic Bacterium Thermus thermophilus Strain HB27

Alexandra Friedrich,1 Christina Prust,2 Thomas Hartsch,3 Anke Henne3, and Beate Averhoff1*

Institut für Genetik und Mikrobiologie, Ludwig-Maximilians-Universität, D-80638 München,1 Abteilung für Allgemeine und Angewandte Mikrobiologie,2 Laboratorium für Genomanalyse (G2L), Institut für Mikrobiologie und Genetik, Georg-August-Universität, D-37077 Göttingen, Germany3

Received 20 August 2001/ Accepted 13 November 2001

Thermus thermophilus HB27, an extremely thermophilic bacterium, exhibits high competence for natural transformation. To identify genes of the natural transformation machinery of T. thermophilus HB27, we performed homology searches in the partially completed T. thermophilus genomic sequence for conserved competence genes. These analyses resulted in the detection of 28 open reading frames (ORFs) exhibiting significant similarities to known competence proteins of gram-negative and gram-positive bacteria. Disruption of 15 selected potential competence genes led to the identification of 8 noncompetent mutants and one transformation-deficient mutant with a 100-fold reduced transformation frequency. One competence protein is similar to DprA of Haemophilus influenzae, seven are similar to type IV pilus proteins of Pseudomonas aeruginosa or Neisseria gonorrhoeae (PilM, PilN, PilO, PilQ, PilF, PilC, PilD), and another deduced protein (PilW) is similar to a protein of unknown function in Deinococcus radiodurans R1. Analysis of the piliation phenotype of T. thermophilus HB27 revealed the presence of single pilus structures on the surface of the wild-type cells, whereas the noncompetent pil mutants of Thermus, with the exception of the pilF mutant, were devoid of pilus structures. These results suggest that pili and natural transformation in T. thermophilus HB27 are functionally linked.

* Corresponding author. Mailing address: Institut für Genetik und Mikrobiologie, Ludwig-Maximilians-Universität, Maria-Ward-Strasse 1a, 80638 Münich, Germany. Phone: 49-89-21806186. Fax. 49-89-21806160. E-mail: B.Averhoff{at}lrz.uni-muenchen.de.

Applied and Environmental Microbiology, February 2002, p. 745-755, Vol. 68, No. 2
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.2.745-755.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lang, E., Haugen, K., Fleckenstein, B., Homberset, H., Frye, S. A., Ambur, O. H., Tonjum, T. (2009). Identification of neisserial DNA binding components. Microbiology 155: 852-862 [Abstract] [Full Text]  
  • Adams, D. G., Duggan, P. S. (2008). Cyanobacteria-bryophyte symbioses. J Exp Bot 59: 1047-1058 [Abstract] [Full Text]  
  • Blas-Galindo, E., Cava, F., Lopez-Vinas, E., Mendieta, J., Berenguer, J. (2007). Use of a Dominant rpsL Allele Conferring Streptomycin Dependence for Positive and Negative Selection in Thermus thermophilus. Appl. Environ. Microbiol. 73: 5138-5145 [Abstract] [Full Text]  
  • Duggan, P. S., Gottardello, P., Adams, D. G. (2007). Molecular Analysis of Genes in Nostoc punctiforme Involved in Pilus Biogenesis and Plant Infection. J. Bacteriol. 189: 4547-4551 [Abstract] [Full Text]  
  • Nakasugi, K., Neilan, B. A. (2005). Identification of Pilus-Like Structures and Genes in Microcystis aeruginosa PCC7806. Appl. Environ. Microbiol. 71: 7621-7625 [Abstract] [Full Text]  
  • Brouns, S. J. J., Wu, H., Akerboom, J., Turnbull, A. P., de Vos, W. M., van der Oost, J. (2005). Engineering a Selectable Marker for Hyperthermophiles. J. Biol. Chem. 280: 11422-11431 [Abstract] [Full Text]  
  • van Schaik, E. J., Giltner, C. L., Audette, G. F., Keizer, D. W., Bautista, D. L., Slupsky, C. M., Sykes, B. D., Irvin, R. T. (2005). DNA Binding: a Novel Function of Pseudomonas aeruginosa Type IV Pili. J. Bacteriol. 187: 1455-1464 [Abstract] [Full Text]  
  • Gil, H., Benach, J. L., Thanassi, D. G. (2004). Presence of Pili on the Surface of Francisella tularensis. Infect. Immun. 72: 3042-3047 [Abstract] [Full Text]  
  • Rossier, O., Starkenburg, S. R., Cianciotto, N. P. (2004). Legionella pneumophila Type II Protein Secretion Promotes Virulence in the A/J Mouse Model of Legionnaires' Disease Pneumonia. Infect. Immun. 72: 310-321 [Abstract] [Full Text]  
  • Friedrich, A., Rumszauer, J., Henne, A., Averhoff, B. (2003). Pilin-Like Proteins in the Extremely Thermophilic Bacterium Thermus thermophilus HB27: Implication in Competence for Natural Transformation and Links to Type IV Pilus Biogenesis. Appl. Environ. Microbiol. 69: 3695-3700 [Abstract] [Full Text]  
  • Igloi, G. L., Brandsch, R. (2003). Sequence of the 165-Kilobase Catabolic Plasmid pAO1 from Arthrobacter nicotinovorans and Identification of a pAO1-Dependent Nicotine Uptake System. J. Bacteriol. 185: 1976-1986 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»