The <i>nik</i> operon of <i>Escherichia coli</i> encodes a periplasmic binding‐protein‐dependent transport system for nickel

Navarro, Clarisse; Wu, Long‐Fei; Mandrand‐Berthelot, Marie‐Andrée

doi:10.1111/j.1365-2958.1993.tb01247.x

Cited by 262 publications

(252 citation statements)

References 46 publications

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“…The addition of nickel to the growth medium specifically restores the intracellular nickel concentration and the hydrogenase activity in this mutant [15][16][17]. In this case, nickel is taken up through the nonspecific magnesium transport system.…”

Section: Effects Of Nickel On the Processing Of The Precursor Of The mentioning

confidence: 91%

“…atives of MC4100 (F-, araD139, A(argF-lac)U169, ptsF25, relA1, flbB5301, rpsL150, deoC1, rbsR, ~,-), are defective in the specific nickel transport system and therefore display a hydrogenase minus phenotype [15][16][17]. Addition of 300 ~M NiC12 to the growth medium results in restoration of the intracellular nickel concentration and hydrogenase activity in this mutant.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Requirement for nickel of the transmembrane translocation of NiFe‐hydrogenase 2 in Escherichia coli

Rodrigue¹,

Boxer

Mandrand‐Berthelot³

et al. 1996

FEBS Letters

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The cellular location of membrane-bound NiFehydrogenase 2 (HYD2) from Escherichia coil was studied by immunobiot analysis and by activity staining. Treatment of spheroplasts with trypsin was able to release active HYD2 into the soluble fraction, indicating that HYD2 is attached to the periplasmic side of the cytoplasmic membrane and that HYD2 undergoes a trans-membrane translocation during its biosynthesis. By using a n/k mutant deficient in the high affinity specific nickel transport system, we show that the intracellniar availability of nickel is essential for the processing of the large subunit and for the transmembrane translocation of HYD2. We also demonstrate that the processing of the precursor, which is related with nickel incorporation, can occur in the membrane-depleted soluble fraction and that it is associated with the increase in resistance to proteolysis of the processed form of the large subunit. The mechanism of the transmembrane translocation of HYD2 is discussed.

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Section: Effects Of Nickel On the Processing Of The Precursor Of The mentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Requirement for nickel of the transmembrane translocation of NiFe‐hydrogenase 2 in Escherichia coli

Rodrigue¹,

Boxer

Mandrand‐Berthelot³

et al. 1996

FEBS Letters

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“…The closest relatives of DBP in E. coli are the oligopeptide- (Guyer et al, 1985;Tame et al, 1994) and nickel-binding (Navarro et al, 1993) proteins, each of which interacts with a different membrane permease. Only the nickel-binding protein has been implicated in chemotaxis, sending signals through a different membrane chemoreceptor than DBP (De Pina et al, 1995).…”

Section: Sequence Comparisonsmentioning

confidence: 99%

“…DBP is a 507-residue periplasmic protein involved in chemotaxis toward, and transport of, many dipeptides and some tripeptides (Manson et al, 1986;Abouhamad et al, 1991;Olson et al, 1991). This protein has also been shown to be related to periplasmic receptors for oligopeptides (Guyer et al, 1985;Tame et al, 1994) and nickel (Navarro et al, 1993). It was particularly striking that proteins so closely related in sequence were implicated in the transport of ligands with such different structures.…”

mentioning

confidence: 99%

Modeling of the structure of the Haemophilus influenzae heme‐binding protein suggests a mode of heme interaction

Dunten¹,

Mowbray²

1995

Protein Science

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The structure and function of the periplasmic heme-binding protein HbpA ofHaemophilus influenzae were investigated. This protein is involved in the import of heme into the bacteria through the inner membrane, and thus is a key element of the organism's ability to survive in blood. A high degree of sequence similarity between HbpA and the dipeptide-binding protein of Escherichia coli is suggested to be the result of a functional relationship. An HbpA model built using the dipeptide-binding protein suggests a mode of heme binding that is distinct from those known in proteins of the human host. These results provide a starting point for rational drug design.Keywords: heme; modeling; periplasmic binding protein; protein structure; transport Haemophilus influenzae is an important cause of meningitis, as well as a major agent of lower respiratory tract and other diseases. The organism has an absolute requirement for exogenously supplied heme, the import of which utilizes a periplasmic lipoprotein, HbpA (Hanson & Hansen, 1991). This heme(haemin)-binding protein is the primary receptor for a heme transport system in the cytoplasmic membrane and, as a key element of the organism's ability to survive in blood, is a desirable target for drugs that would inhibit heme transport. As part of a transport system, it could also be used as a means of selective delivery of toxic compounds into the bacterial cell. The sequence is strongly conserved among various Haemophilus strains (Hanson et al., 1992). A similar protein has also been found in Yersinia enterocolitica (Stojiljkovic & Hantke, 1994) and proposed to exist in Neisseria meningitidis (Stojiljkovic et al., 1995), other hemerequiring pathogens. These facts suggest that drugs aimed at HbpA might be generally useful for a variety of disease-causing bacteria. The success of such a strategy depends largely on the ability to design drugs that do not interfere with the normal roles of heme in the host, and thus also on a knowledge of the modes of heme binding in the protein structures involved. The X-ray Reprint requests to: Sherry L. Mowbray, Department of Molecular Biology, BioMedical Center, Box 590, Swedish University of Agricultural Sciences, 75124 Uppsala, Sweden; e-mail: mowbray@xray.bmc.uu.se.Abbreviations: HbpA, the heme-binding protein of Haemophilus influenzae; DBP, the dipeptide-binding protein of Escherichia coli.

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“…This variation in residues might reflect the fact that several of these binding proteins do not bind peptides. For instance, heme is bound by HbpA of Haemophilus influenzae [20], agrocinopines by AccA of Agrobacterium tumefaciens [22], and nickel by NikA of E. coli (table II, [36]). …”

Section: Sequence Comparison Of Oligopeptide Binding Proteinsmentioning

confidence: 99%

Peptides and ATP binding cassette peptide transporters

Detmers

Lanfermeijer

Poolman

2001

Research in Microbiology

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-In this review our knowledge of ATP binding cassette (ABC) transporters specific for peptides is discussed. Besides serving a role in nutrition of the cell, the systems participate in various signaling processes that allow (micro)organisms to monitor the local environment. In bacteria, these include regulation of gene expression, competence development, sporulation, DNA transfer by conjugation, chemotaxis, and virulence development, and the role of ABC transporters in each of these processes is discussed. Particular attention is paid to the specificity determinants of peptide receptors and transporters in relation to their structure and to the mechanisms of peptide binding.

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The nik operon of Escherichia coli encodes a periplasmic binding‐protein‐dependent transport system for nickel

Cited by 262 publications

References 46 publications

Requirement for nickel of the transmembrane translocation of NiFe‐hydrogenase 2 in Escherichia coli

Requirement for nickel of the transmembrane translocation of NiFe‐hydrogenase 2 in Escherichia coli

Modeling of the structure of the Haemophilus influenzae heme‐binding protein suggests a mode of heme interaction

Peptides and ATP binding cassette peptide transporters

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