scholarly journals Identification of genes involved in siderophore transport inStreptomyces coelicolorA3(2)

2006 ◽  
Vol 262 (1) ◽  
pp. 57-64 ◽  
Author(s):  
Robert Bunet ◽  
Anita Brock ◽  
Hans-Ulrich Rexer ◽  
Eriko Takano
2001 ◽  
Vol 183 (20) ◽  
pp. 5885-5895 ◽  
Author(s):  
S. Peter Howard ◽  
Christina Herrmann ◽  
Chad W. Stratilo ◽  
V. Braun

ABSTRACT The siderophore transport activities of the two outer membrane proteins FhuA and FecA of Escherichia coli require the proton motive force of the cytoplasmic membrane. The energy of the proton motive force is postulated to be transduced to the transport proteins by a protein complex that consists of the TonB, ExbB, and ExbD proteins. In the present study, TonB fragments lacking the cytoplasmic membrane anchor were exported to the periplasm by fusing them to the cleavable signal sequence of FecA. Overexpressed TonB(33-239), TonB(103-239), and TonB(122-239) fragments inhibited transport of ferrichrome by FhuA and of ferric citrate by FecA, transcriptional induction of the fecABCDE transport genes by FecA, infection by phage φ80, and killing of cells by colicin M via FhuA. Transport of ferrichrome by FhuAΔ5-160 was also inhibited by TonB(33-239), although FhuAΔ5-160 lacks the TonB box which is involved in TonB binding. The results show that TonB fragments as small as the last 118 amino acids of the protein interfere with the function of wild-type TonB, presumably by competing for binding sites at the transporters or by forming mixed dimers with TonB that are nonfunctional. In addition, the interactions that are inhibited by the TonB fragments must include more than the TonB box, since transport through corkless FhuA was also inhibited. Since the periplasmic TonB fragments cannot assume an energized conformation, these in vivo studies also agree with previous cross-linking and in vitro results, suggesting that neither recognition nor binding to loaded siderophore receptors is the energy-requiring step in the TonB-receptor interactions.


2005 ◽  
Vol 187 (2) ◽  
pp. 422-433 ◽  
Author(s):  
Carey A. Kunkle ◽  
Michael P. Schmitt

ABSTRACT This report describes a genetic locus associated with siderophore biosynthesis and transport in Corynebacterium diphtheriae. A BLAST search of the C. diphtheriae genome identified a seven-gene cluster that included four genes, designated ciuA, ciuB, ciuC, and ciuD, whose predicted products are related to ABC-type iron transporters. Downstream from ciuD is the ciuE gene, whose predicted product is similar to the aerobactin biosynthetic enzymes IucA and IucC. The CiuE protein, which has a predicted mass of 121,582 Da and is approximately twice the size of either IucC or IucA, is homologous to each of these proteins in both its N- and C-terminal regions. C. diphtheriae ciuE deletion mutants exhibited a defect in siderophore production, iron uptake, and growth in low-iron medium. Mutations in the ciuA gene, whose predicted product is a lipoprotein component of an iron transport system, resulted in a severe defect in iron uptake and reduced ability to use the C. diphtheriae siderophore as an iron source. Site-directed mutations in irp6A, a gene previously reported to be associated with siderophore transport, had no effect on iron uptake or the utilization of the C. diphtheriae siderophore as an iron source. Transcriptional analysis demonstrated that expression of ciuA and ciuE is DtxR and iron regulated, and DNase I protection experiments confirmed the presence of DtxR binding sites upstream from each of these genes. Thus, this iron- and DtxR-regulated gene cluster is involved in the synthesis and transport of the C. diphtheriae siderophore.


2006 ◽  
Vol 110 (9) ◽  
pp. 1102-1110 ◽  
Author(s):  
Elena LÓPEZ-ERRASQUÍN ◽  
M. Teresa GONZÁLEZ-JAÉN ◽  
Carmen CALLEJAS ◽  
Covadonga VáZQUEZ

1985 ◽  
Vol 162 (2) ◽  
pp. 715-721 ◽  
Author(s):  
H Huschka ◽  
H U Naegeli ◽  
H Leuenberger-Ryf ◽  
W Keller-Schierlein ◽  
G Winkelmann

2005 ◽  
Vol 280 (34) ◽  
pp. 30574-30580 ◽  
Author(s):  
H. Anne Eisenhauer ◽  
Sofia Shames ◽  
Peter D. Pawelek ◽  
James W. Coulton

2007 ◽  
Vol 189 (9) ◽  
pp. 3479-3488 ◽  
Author(s):  
Michiel Stork ◽  
Manuela Di Lorenzo ◽  
Timothy J. Welch ◽  
Jorge H. Crosa

ABSTRACT The iron transport-biosynthesis (ITB) operon in Vibrio anguillarum includes four genes for ferric siderophore transport, fatD, -C, -B, and -A, and two genes for siderophore biosynthesis, angR and angT. This cluster plays an important role in the virulence mechanisms of this bacterium. Despite being part of the same polycistronic mRNA, the relative levels of transcription for the fat portion and for the whole ITB message differ profoundly, the levels of the fat transcript being about 17-fold higher. Using S1 nuclease mapping, lacZ transcriptional fusions, and in vitro studies, we were able to show that the differential gene expression within the ITB operon is due to termination of transcription between the fatA and angR genes, although a few transcripts proceeded beyond the termination site to the end of this operon. This termination process requires a 427-nucleotide antisense RNA that spans the intergenic region and acts as a novel transcriptional terminator.


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