Disease relevance of skp

• Identity of the 17-kilodalton protein, a DNA-binding protein from Escherichia coli, and the firA gene product [1].
• We have recently described a previously uncharacterized outer membrane protein of Salmonella typhimurium and Escherichia coli and cloned and sequenced the corresponding gene, the ompH gene, of S. typhimurium (P. Koski, M. Rhen, J. Kantele, and M. Vaara, J. Biol. Chem. 264:18973-18980, 1989) [2].
• The ompH gene of Yersinia enterocolitica: cloning, sequencing, expression, and comparison with known enterobacterial ompH sequences [2].
• Escherichia coli skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments [3].
• Cloning and characterization of the major outer membrane protein gene (ompH) of Pasteurella multocida X-73 [4].

High impact information on skp

• The Seventeen Kilodalton Protein (Skp) is a trimeric periplasmic chaperone that assists outer membrane proteins in their folding and insertion into membranes [5].
• Coexpression of skp also increases the functional yield of scFv fragments when expressed by secretion to the periplasm [6].
• We used the well-characterized P pilus biogenesis system in Escherichia coli as a model to elucidate the mechanism of action of a periplasmic chaperone, PapD, which is specifically required for P pilus biogenesis [7].
• The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane [8].
• Pulse labeling of OmpA in spheroplasts prepared from an skp null mutant revealed a specific requirement of Skp for the release of newly translocated outer membrane proteins from the plasma membrane [9].

Chemical compound and disease context of skp

• A complex of the periplasmic chaperone FimC and the mannose-binding adhesin FimH from the Escherichia coli type 1 pilus system has been crystallized from ammonium sulfate solution using the hanging-drop vapour-diffusion method [10].
• Addition of DsbC, replacing polyethylene glycol with spermidine and putrescine to create a more natural environment, adding Skp, an E. coli periplasmic chaperone, and expressing PA at 30 degrees C increased the solubility of the protein product as well as the yield of active PA [11].

Biological context of skp

• The nucleotide sequence similarity between the corresponding genes hlpA and ompH is 87% [12].
• The HlpA protein which is encoded by the hlpA gene in the plastid genome of the cryptomonad alga Chryptomonas phi is structurally related to the non-sequence-specific DNA-binding and DNA-bending HU family of chromatin-associated proteins [13].
• The ompH gene is located in a gene cluster resembling the hlpA-ORF17 region of E. coli which is close to the Ipx genes involved in the biosynthesis of lipopolysaccharides [12].
• An E. coli transformant containing the skp gene on the plasmid pGAH317 was shown to overproduce the gene product some 20-fold [14].
• It is significantly homologous to the ompH genes of E. coli and S. typhimurium (homology percentages, 65 and 64%, respectively), has a promoter region strongly homologous to the E. coli 17-bp class consensus promoter, and encodes a protein consisting of 165 amino acids (22 of which form the signal sequence) [2].

Anatomical context of skp

• The recombinant product of the Chryptomonas phi plastid gene hlpA is an architectural HU-like protein that promotes the assembly of complex nucleoprotein structures [13].

Associations of skp with chemical compounds

• The NH2-terminal 35 amino acids were found to be identical to those of the skp (firA) gene product, to which several putative functions have previously been attributed [15].
• Periplasmic chaperone LolA formed a complex with the released L10P(DQ), which was subsequently incorporated into the outer membrane in a LolB-dependent manner, indicating that neither LolA nor LolB rejects lipoproteins with aspartate at position 2 [16].
• By construction of a P. multocida fur mutant, it has been demonstrated that the ompH gene, encoding a major structural protein of the outer membrane, presenting high antigenicity power, is negatively regulated by iron and glucose [17].

Other interactions of skp

• However, nine acid-inducible genes are clustered in the gadA region, including hdeA, which encodes a putative periplasmic chaperone, and four putative regulatory genes [18].
• The LolA protein, a periplasmic chaperone functioning as an outer-membrane lipoprotein carrier of the Lol system which mediates translocation of the water-insoluble outer-membrane lipoprotein across the periplasm in Gram-negative bacteria, was crystallized in two forms: orthorhombic (I222) and trigonal (P3(1)21 or P3(2)21) [19].

Analytical, diagnostic and therapeutic context of skp

• Furthermore, we isolated by molecular cloning the corresponding gene, named it ompH, and determined its nucleotide sequence [20].
• Screening of the library against the bacterial periplasmic chaperone PapD was performed using surface plasmon resonance [21].
• The ability of the peptides to inhibit the protein-protein interaction between the periplasmic chaperone FimC and the pilus adhesin FimH was then determined in an ELISA [22].
• The gene (ompH) encoding OmpH has been isolated and sequenced by construction of a genomic library and PCR techniques [4].

References