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Sequence Common to All Tonb-Dependent Outer Membrane JOURNAL OF BACTERIOLOGY, May 1987, p. 2044-2049 Vol. 169, No. 5 0021-9193/87/052044-06$02.00/0 Copyright © 1987, American Society for Microbiology Feric-Coprogen Receptor FhuE of Escherichia coli: Processing and Sequence Common to all TonB-Dependent Outer Membrane Receptor Proteins MARTIN SAUER, KLAUS HANTKE, AND VOLKMAR BRAUN* Mikrobiologie II, Universitat Tubingen, D-7400 Tubingen, Federal Republic of Germany Received 9 September 1986/Accepted 6 February 1987 Iron transport via siderophores requires outer membrane receptor proteins and the TonB protein. The FhuE protein of Escherichia coli functions as the receptor for ferric coprogen and ferric-rhodotorulic acid. A chromosomal DNA fragment bearing the flauE gene was cloned into pACYC184. The gene was localized by insertion mutagenesis by using the transposon TnlOOO. Expression in minicells revealed a FhuE precursor with an apparent molecular weight of 82,000 and a FhuE protein with a molecular weight of 76,000. The transcription polarity of the JIuE gene was deduced from the size of truncated polypeptides derived from Tn1000 insertions, which were mapped by restriction analysis. The processing of truncated precursors that were synthesized by insertion mutants was strongly reduced even when the insertion site was close to the carboxy terminus of the FhuE protein. It is concluded that either the efficent insertion of proFhuE into the cytoplasmic membrane or the rate of cleavage of the signal peptide requires a particular conformation of the proFhuE protein, which is only formed by the complete primary structure. The amino-terminal amino acid sequence deduced from the nucleotide sequence was confirmed by gas-phase sequencing of the precursor and the mature form, which were separated by electrophoresis on polyacrylamide gels. The precursor contained an unusually long signal peptide of 36 amino acids. The amino-terminal end of the mature form contained the sequence Glu-Thr-Val-Ile-Val. A pentapeptide starting with either Glu or Asp, followed by Thr, and two uncharged residues ending with Val were found in all outer membrane receptor proteins that were constituents of TonB-dependent transport systems. From results of studies concerning the energy requirement this sequence forms the binding domain for the TonB pro- and TonB dependence of the irreversible adsorption of tein. phages Ti and 480 to Escherichia coli cells, we concluded in Transport systems for five ferric-siderophore compounds 1976 (14) that the function determined by the tonB region have been identified in E. coli (for recent reviews, see may be to couple the energized state of the cytoplasmic references 6 and 26). One of these siderophores is coprogen membrane to the TonA outer membrane receptor protein. B, which is formed by Neurospora crassa and by certain Later it was shown that ligands did bind to their receptors in Penicillium species (20). The existence ofa specific transport unenergized cells or in tonB mutants but remained there and system for coprogen was deduced from the discovery of an were not translocated across the outer membrane (7, 18, 32). outer membrane receptor protein, designated FhuE (17). In some cases the requirement for the outer membrane Mutants in flzuE were defective in the transport of iron receptor protein for uptake could be bypassed by osmotic delivered as coprogen or as a complex with rhodotorulic shock (7) or by the preparation of spheroplasts (36). Under acid, which is another metabolite of certain fungi. In both these conditions the TonB function was no longer needed, siderophores hydroxamate groups serve as the iron-binding suggesting that it was indeed involved in the translocation of sites. Consistent with other hydroxamate siderophores (e.g., iron siderophores (12, 15), vitamin B12 (3, 32), and the aerobactin, ferrichrome), ferric coprogen and rhodotorulic B-group colicins (31) across the outer membrane. Despite acid bind to specific outer membrane receptor proteins, this consistent evidence in favor of the original proposal, while subsequent transport steps are catalyzed by common direct proof of a physical interaction between the TonB genes,flzuB,fluC,fluD, tonB, and exbB (11, 17). protein (25, 28-30) and outer membrane receptor proteins is To determine whether the FhuE protein also contains the lacking. homology region at the amino-terminal end common to all Recently, the nucleotide sequences of the structural genes TonB-dependent receptor proteins, we cloned the gene and for the receptors of vitamin B12 (19), ferric aerobactin (21), sequenced this region. Moreover, we found an unusually ferrichrome (9; R. Burkhardt, unpublished data), and ferric long signal peptide and a rather slow processing rate of the enterochelin (23) were determined. They all possess a con- FhuE precursor. sensus sequence near the amino-terminal end of the mature proteins. A mutant in vitamin B12 transport, which still MATERIALS AND METHODS adsorbed a normal amount of vitamin B12 with unaltered affinity, apparently was defective in the vectorial release of Bacterial strains and media. The E. coli K-12 strains used vitamin B12 from the receptor into the periplasm. In this in this study are listed in Table 1. For the isolation of the mutant a leucine residue was replaced by a proline residue fhuE: :A plac Mu53 mutant JB1690, strain MC4100 was within the consensus sequence (19). It was suggested that infected with X plac Mu53 (8). Neomycin-resistant colonies were isolated. These colonies were red on MacConkey plates containing 50 ,uM 2,2'-dipyridyl. To determine lacZ * Corresponding author. expression under the control of an iron-regulated operator, 2044 VOL. 169, 1987 FERRIC-COPROGEN RECEPTOR PROTEIN OF E. COLI 2045 TABLE 1. E. coli K-12 strains used in this study inserts in the JhuE gene of pKH6 were screened on NBD Source of plates, which were supplemented with 0.2 mM Fe3+- Strain Genotype reference Desferal and 40 pLg of chloramphenicol per ml. fhuE+ strains CR63 F+ Universitat formed larger colonies on Fe3+-ferrioxamine B than didffhuE Tubingen mutant strains. The plasmids were isolated from 16 conju- MC4100 F- araD139 A1acUl69 rpsL150 relAl M. Casada- gants that formed very small colonies and were designated flbBS301 deoCI ptsF25 rbsR ban MS1 to MS16. They were cleaved with the enzymes Sail, H1443 As MC4100, but aroB 17 HindlIl, PvuII, and KpnI to determine the insertion sites and H1619 As H1443, but JhuE::Mu dlX This study the orientation of TnJOOO. H1729 As H1443, but cirfhuA fiu::Mu dlX This study Tabor and Richardson (34) constructed vectors in which JB1690 As MC4100, butjhuE::X plac Mu53 This study inserted genes are transcribed by the T7 polymerase under DS410 minA minB rpsL lacY xyl thi mtl 10 the control of a T7 promoter. The plasmid pT7 6 contains a JM101 supE thi A(lac proAB) (F, traD36 37 the proAB lacIq lac ZM15) polylinker preceded by promoter of the T7 gene 10. In IR20/111 aroB cirfhuA fepA malA Universitat addition, they contain the bla gene with a transcription Tubingen polarity opposite to that of the 4i10 promoter region (S. MS44 As IR20/111, but containing pGPl-2 This study Tabor, private communication). The 6.7-kilobase (kb) and pMS44 HindIII-EcoRI fragment of pKH6 was cloned into pT7-6 MS50 As H1729, but containing pKH6 This study digested with HindIII-EcoRI. Ampicillin-resistant trans- MS172 As H1443, but containingfluE::X This study formants of E. coli H1443 were screened, and plasmids were plac Mu53 reisolated and tested for the expected insert by restriction MS200 As DS410, but containing pKH6 This study analysis. The resulting plasmid pMS44 was transferred into MS201-211 As DS410, but containing pMS1-11 This study E. coli IR20/111 which was transformed earlier by pGP1-2, WM1576 HfrC lambda carrying pGPl-2 34 which was isolated from E. coli WM1576. An ampicillin- and neomycin-resistant derivative was designated E. coli MS44. Recombinant DNA techniques. Digestion with restriction the red colonies were cross-streaked onto MacConkey plates enzymes was performed by the method described by that contained 50 ,uM Fe3+, and then onto these plates was Maniatis et al. (24) or as recommended by the supplier placed a paper strip that was impregnated with 20 mM (Boehringer GmbH, Mannheim, Federal Republic of Ger- 2,2'-dipyridyl. The dipyridyl diffused from the paper strip many). Plasmids were isolated as described by Birnboim (5). into the agar and formed a gradient of iron deficiency. DNA was treated with RNase and then with proteinase K Colonies that were red near the paper strip and white further (24). For purification of DNA by CsCl gradient centrifuga- away contained lacZ under iron regulation (16). Mutants in tion, the ethanol precipitate of DNA of a 1-liter culture was ffhuE were selected on the basis of no growth stimulation by dissolved in 2.4 ml of 10 mM Tris hydrochloride-1 mM coprogen B on iron-deficient NBD plates (8 g of nutrient EDTA (pH 7.5, TE buffer). Cesium chloride (4.2 g) and 0.4 broth, 5 g of NaCl per liter, 0.2 mM 2,2'-dipyridyl). To ml of ethidium bromide (10 mg/ml) were added. This solution exclude mutants in fhuB, fhuC, flhuD, tonB, and exbB, was layered below 8 ml of CsCl (6.4 g in 10 ml of TE buffer) growth stimulation by ferrichrome, the uptake system of and then centrifuged for 4.5 h at 65,000 x g. which shares these genes with the coprogen uptake system, DNA was sequenced by the enzymatic method (33, 37) by was tested. Mutants in fhuE were also albomycin sensitive, using [35S]dATP for labeling (4) and the M13-sequencing kit whereas Jfhu mutants have been shown to be albomycin from Amersham Buchler, Braunschweig, Federal Republic resistant (11, 26). Growth promotion was tested around filter of Germany.
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