Appl Environ Microbiol 2009, 75:7537–41 PubMedCrossRef 61 Huber

Appl Environ Microbiol 2009, 75:7537–41.PubMedCrossRef 61. Huber T, Faulkner G, Hugenholtz P: Bellerophon: a program to detect chimeric sequences in multiple sequence alignments. [http://​greengenes.​lbl.​gov/​cgi-bin/​nph-bel3_​interface.​cgi] Bioinformatics 2004, 20:2317–2319.PubMedCrossRef 62. Rambaut A: FigTree. [http://​tree.​bio.​ed.​ac.​uk/​software] 63. Ciardo Mizoribine DE, Schar G, Altwegg M, Bottger EC, Bosshard PP: Identification

of moulds in the diagnostic laboratory–an algorithm implementing molecular and phenotypic methods. Diagn Microbiol Infect Dis 2007, 59:49–60.PubMedCrossRef 64. Colwell RK: EstimateS: Statistical estimation of species richness and shared species from samples. [http://​purl.​oclc.​org/​estimates] 65. R Development Core Team: R: A language and environment for statistical computing. [http://​www.​R-project.​org] Vienna: R Foundation for Statistical Computing; 2008. 66. Lozupone C, Hamady M, Knight R: UniFrac–an online tool for comparing microbial community diversity in a phylogenetic context. [http://​bmf.​colorado.​edu/​unifrac/​] 4SC-202 chemical structure BMC Bioinformatics 2006, 7:371.PubMedCrossRef Authors’ contributions MP did the cloning, sequencing and data-analyses

and drafted the manuscript, TM performed the qPCR assays and edited the manuscript, AH did the ergosterol analyses and edited the manuscript, AN designed the study and edited the manuscript, LP participated in study designing and supervised the sequencing, PA edited the manuscript, UL did the culture analyses and edited the manuscript, HR collected the samples, performed the qPCR assays and edited the manuscript. All authors participated in the study design and read and approved the final

manuscript.”
“Background The Ferric uptake regulator (Fur) is a metal-dependent regulator of transcription and post-transcription in bacteria, which senses metal concentration and/or the redox state of the cells (reviewed in [1]). The classical model of the regulatory role of Fur depicts transcriptional repression through ferrous iron that results in Fur-Fe2+ Fosbretabulin order binding to the operator site of a target gene [2, 3]. Fur-Fe2+ binding to DNA are presumed to be homodimeric; however, multimeric complexes have been reported [4, 5]. In addition, the metal Bacterial neuraminidase cofactor present in vivo is controversial, due to the ability of the Fur protein to bind different divalent cations, in vitro [6]. For example, Fur represses aerobactin biosynthesis using ferrous iron, cobalt, or manganese [2]. Moreover, most researchers studying Fur binding to promoter sequences, in vitro, employ manganese instead of ferrous iron due to the reactivity of ferrous iron with oxygen. However, evidence exists that Fur regulates specific genes differently in the presence of ferrous iron or manganese [7]. Fur also contains zinc for protein stability [8, 9]. This indicates that the availability of the metal cofactor to pathogens residing in the host dictates the activity of Fur.

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