Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins

Speiser, David M.; Ames, Giovanna Ferro‐Luzzi

doi:10.1128/jb.173.4.1444-1451.1991

Cited by 63 publications

(52 citation statements)

References 26 publications

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“…The existence of such a site in HisQMP 2 has been suggested by the properties of receptor-independent mutants (32,35), the inhibition of in vitro transport by histidine trapped inside PLS (6), and the altered substrate specificity of several strains carrying mutations in either HisQ or HisM (31). The function of this postulated site might be to bind the histidine released from liganded HisJ and initiate a series of conformational changes required for trans- b IC 50 is the concentration which gives 50% inhibition in the presence of 2 mM ATP.…”

Section: Permeabilization Of Pls Is Necessary Tomentioning

confidence: 99%

Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

Liu

Ames

1997

Journal of Biological Chemistry

116

122

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The superfamily of traffic ATPases (ABC transporters) includes bacterial periplasmic transport systems (permeases) and eukaryotic transporters. The histidine permease of Salmonella typhimurium is composed of a membrane-bound complex (HisQMP 2 ) containing four subunits, and of a soluble receptor, the histidine-binding protein (HisJ). Transport is energized by ATP. In this article the ATPase activity of HisQMP 2 has been characterized, using a novel assay that is independent of transport. The assay uses Mg 2؉ ions to permeabilize membrane vesicles or proteoliposomes, thus allowing access of ATP to both sides of the bilayer. HisQMP 2 displays a low level of intrinsic ATPase activity in the absence of HisJ; unliganded HisJ stimulates the activity and liganded HisJ stimulates to an even higher level. All three levels of activity display positive cooperativity for ATP with a Hill coefficient of 2 and a K 0.5 value of 0.6 mM. The activity has been characterized with respect to pH, salt, phospholipids, substrate, and inhibitor specificity. Free histidine has no effect.

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Section: Permeabilization Of Pls Is Necessary Tomentioning

confidence: 99%

Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

Liu

Ames

1997

Journal of Biological Chemistry

116

122

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“…This protein acts as a receptor and is required for high affinity substrate import (10). In mutant ABC systems, which no longer require the solute-binding protein for substrate import, substrate specificity is maintained due to binding sites located in the TMD component of the transporter (11)(12)(13). The solute-binding proteins are believed to play an additional role in transport by transmitting a signal across the membrane, thus stimulating ATP hydrolysis by the NBD subunits (14,15).…”

mentioning

confidence: 99%

The C-terminal Domain of the Nucleotide-binding Domain Protein Wzt Determines Substrate Specificity in the ATP-binding Cassette Transporter for the Lipopolysaccharide O-antigens in Escherichia coli Serotypes O8 and O9a

Cuthbertson¹,

Powers²,

Whitfield

2005

Journal of Biological Chemistry

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The polymannan O-antigenic polysaccharides (O-PSs) of Escherichia coli O8 and O9a are synthesized via an ATP-binding cassette (ABC) transporter-dependent pathway. The group 2 capsular polysaccharides of E. coli serve as prototypes for polysaccharide synthesis and export via this pathway. Here, we show that there are some fundamental differences between the ABC transporter-dependent pathway for O-PS biosynthesis and the capsular polysaccharide paradigm. In the capsule system, mutants lacking the ABC transporter are viable, and membranes isolated from these strains are no longer able to synthesize polymer using an endogenous acceptor. In contrast, E. coli strains carrying mutations in the membrane component (Wzm) and/or the nucleotide-binding component (Wzt) of the O8 and O9a polymannan transporters are nonviable under conditions permissive to O-PS biosynthesis and take on an aberrant elongated cell morphology. Whereas the ABC transporters for capsular polysaccharides with different structures are functionally interchangeable, the O8 and O9a exporters are specific for their cognate polymannan substrates. The E. coli O8 and O9a Wzt proteins contain a C-terminal domain not present in the corresponding nucleotide-binding protein (KpsT) from the capsule exporter. Whereas the Wzm components are functionally interchangeable, albeit with reduced efficiency, the Wzt components are not, indicating a specific role for Wzt in substrate specificity. Chimeric Wzt proteins were constructed in order to localize the region involved in substrate specificity to the C-terminal domain. ATP-binding cassette (ABC)1 transporters, or traffic ATPases, are responsible for the import and export of a variety of molecules across membranes. In the Escherichia coli K-12 genome, 79 known or putative ABC transporters have been identified indicating the importance of this protein superfamily in cellular physiology (1). The prototypical transporter consists of four domains (two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs)), which may be organized in a variety of ways (2). The TMD components between different systems share low sequence similarity and contain a variable number of transmembrane segments, whereas the NBD proteins of different systems share a higher overall sequence similarity as a result of the conserved sequence motifs required for ATP hydrolysis (3). X-ray structures are available for a number of NBD proteins as well as four complete transporters (reviewed in Refs. 4 -7). The structures reveal a common organization of the NBD monomers into two subdomains: a RecAlike domain and a helical domain not found in other ATPhydrolyzing proteins (4). The ATP-binding site is found along the NBD dimer interface and is made up of conserved residues from each monomer, namely the Walker A motif from one monomer and the ABC signature motif from the other monomer (8). Because the ABC transporter TMD components differ greatly between systems, whereas the NBD components remain highly similar, ABC transporters have been said to...

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“…Translocation is energized by FhuC-catalyzed ATP hydrolysis, which induces a conformational change in FhuB (22 (31) and suppress transport-defective hisJ mutations (3,29).…”

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confidence: 99%

Iron(III) hydroxamate transport in Escherichia coli K-12: FhuB-mediated membrane association of the FhuC protein and negative complementation of fhuC mutants

et al. 1992

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Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins

Cited by 63 publications

References 26 publications

Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

The C-terminal Domain of the Nucleotide-binding Domain Protein Wzt Determines Substrate Specificity in the ATP-binding Cassette Transporter for the Lipopolysaccharide O-antigens in Escherichia coli Serotypes O8 and O9a

Iron(III) hydroxamate transport in Escherichia coli K-12: FhuB-mediated membrane association of the FhuC protein and negative complementation of fhuC mutants

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