Disease relevance of gltF

• gltF, a member of the gltBDF operon of Escherichia coli, is involved in nitrogen-regulated gene expression [1].
• Roles of glutamate synthase, gltBD, and gltF in nitrogen metabolism of Escherichia coli and Klebsiella aerogenes [2].
• Heme, a major iron source, is transported through the outer membrane of Gram-negative bacteria by specific heme/hemoprotein receptors and through the inner membrane by heme-specific, periplasmic, binding protein-dependent, ATP-binding cassette permeases [3].
• The protein contains the sequence Cys-Pro-His-Cys (CPHC) and is highly similar to two other periplasmic CPHC motif-containing proteins: DsbA, an Escherichia coli protein (45% identity, 87% homology) and TcpG, a Vibrio cholerae protein (32% identity, 74% homology) [4].
• A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd [4].

High impact information on gltF

• Oxidation of cysteine pairs to disulfide requires cellular factors present in the bacterial periplasmic space [5].
• DsbB is an E. coli membrane protein that oxidizes DsbA, a periplasmic dithiol oxidase [5].
• Together with the previous contention that the Cpx system senses a protein abnormality not only at periplasmic and outer membrane locations but also at the plasma membrane, abnormal states of membrane proteins are postulated to be generated in these secY mutants [6].
• The mutations did not interfere with the biogenesis of the protein, and disulfide bond formation appeared to be dependent on the periplasmic enzyme DsbA, which catalyzes disulfide bond formation in the periplasm [7].
• Remarkably, in the presence of ligand, increased reactivity is observed with Cys replacements located predominantly on the periplasmic side of the sugar-binding site [8].

Chemical compound and disease context of gltF

• The excC mutants of Escherichia coli are hypersensitive to drugs such as cholic acid and release periplasmic proteins into the extracellular medium [9].
• The physiological role of the periplasmic nitrate reductase, Nap, one of the three nitrate reductases synthesized by Escherichia coli K-12, has been investigated [10].
• Hence, utilizing a constructed cDNA library from the venom glands of the black mamba (Dendroaspis polylepis), the gene encoding dendrotoxin K was isolated, amplified, and expressed as a maltose-binding fusion protein in the periplasmic space of Escherichia coli [11].
• DsbC is a periplasmic protein of Escherichia coli that was previously identified by a genetic selection that rescued sensitivity to dithiothreitol in Tn10 mutagenized cells [12].
• Murein endopeptidase A (MepA) from Escherichia coli is a periplasmic peptidoglycan amidase that cleaves d,d amide bonds between d-alanine and meso-2,6-diaminopimelic acid in E. coli peptidoglycan [13].

Biological context of gltF

• Third, glutamate-dependent repression of the glt operon appears to be mediated by the product of the gltF gene [1].
• Two open reading frames were identified, the first of which corresponds to gltF [1].
• Here, we show that to use heme iron E. coli requires the dipeptide inner membrane ATP-binding cassette transporter (DppBCDF) and either of two periplasmic binding proteins: MppA, the L-alanyl-gamma-D-glutamyl-meso-diaminopimelate binding protein, or DppA, the dipeptide binding protein [3].
• Together, our data support a model in which SurA is specialized to interact with non-native periplasmic outer membrane protein folding intermediates and to assist in their maturation from early to late outer membrane-associated steps [14].
• These results identify the first prokaryotic GSH transporter and indicate a key role for GSH in periplasmic redox homeostasis [15].

Anatomical context of gltF

• The most striking feature of the AcrB trimer is the presence of three vestibules open to the periplasm at the boundary between the periplasmic headpiece and the transmembrane region [16].
• Whereas newly synthesized lipoproteins could be released from spheroplasts of Escherichia coli upon addition of a periplasmic extract containing LolA, de novo synthesized LPS was not released [17].
• These results suggest that periplasmic inclusion body formation may result in intermolecular interactions between participating proteins without loss of function of the fused enzymes [18].
• The resultant periplasmic extract lacked lipopolysaccharide, protein markers of inner or outer membranes, surface-radiolabelled protein components, or ribosomal proteins [19].
• The secretion of the alpha-haemolysin is mediated by the type I secretion system and the toxin reaches the extracellular space without the formation of periplasmic intermediates presumably in a soluble form [20].

Associations of gltF with chemical compounds

• The second transport system, whose structural gene was called gltF and is located at minute 0, was L-glutamate specific, sodium independent, and alpha-methylglutamate sensitive [21].
• Saccharomyces cerevisiae strains able to use sucrose produce the enzyme invertase, which is targeted by a signal peptide to the central secretory pathway and the periplasmic space [22].
• After isopropyl beta-D-thiogalactoside induction, the 70-kDa His(10)-tagged m22(scFv)-ETA' was directed into the periplasmic space and purified by a combination of metal-ion affinity and molecular size-chromatography [23].
• Indeed, the C domain probably extends well beyond the confines of the outer membrane bilayer, forming a centrally plugged channel that penetrates both the peptidoglycan on the periplasmic side and the lipopolysaccharide and capsule layers on the cell surface [24].
• The membrane-bound complex of the prokaryotic histidine permease, a periplasmic protein-dependent ABC transporter, is composed of two hydrophobic subunits, HisQ and HisM, and two identical ATP-binding subunits, HisP, and is energized by ATP hydrolysis [25].

Other interactions of gltF

• First, insertions in gltB, gltD or gltF all prevent Ntr induction [1].
• The glt operon of Escherichia coli comprises the structural genes for the glutamate synthase subunits (gltB and gltD) and gltF, whose product was previously suggested to have regulatory functions [26].
• Cloning and expression of Vibrio cholerae dsbA, a gene encoding a periplasmic protein disulphide isomerase [27].

Analytical, diagnostic and therapeutic context of gltF

• Moreover, two-dimensional gel electrophoresis revealed that the production of two periplasmic proteins, PotD and OppA, is increased in E. coli cells under ColE7 exposure [28].
• The periplasmic location of the amino terminus was confirmed by immunoelectron microscopy of spheroplasts from F' and pTG801 strains, using a monoclonal antibody that recognizes an amino-terminal epitope [29].
• The pore constriction and the periplasmic outlet are very similar to OmpF with 74% of the pore lining residues being conserved [30].
• All tested constructs gave rise to abundant periplasmic expression of pallidipin, which was then purified by a combination of cation- and anion-exchange chromatography followed by size-exclusion gel chromatography [31].
• Lipid-layer crystallization and preliminary three-dimensional structural analysis of AcrA, the periplasmic component of a bacterial multidrug efflux pump [32].

References