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Osteogenesis imperfecta type IV: evidence of abnormal triple helical structure of type I collagen 总被引:4,自引:0,他引:4
Summary Skin fibroblasts from a patient with mild osteogenesis imperfecta (OI) type IV synthesize two populations of type I procollagen molecules. One population contains pro1(I) and pro2(I) chains that migrate normally in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and a second population contains only slower migrating pro1(I) and pro2(I) chains. The total amount of type I procollagen made by OI cells and the ratio of pro1(I): pro2(I) is normal. When labeled under conditions that inhibit post-translational modification of pro chains, the OI cells produce only single populations of pro1(I) and pro2(I) chains indicating that the apparent increased molecular weight of some OI pro chains is due to excessive post-translational modification rather than peptidyl insertions. Peptide maps indicate that excessive post-translational modification occurs along the entire triple helical segment of some 1(I) and 2(I) chains produced by OI cells. The effect of the mutation is to lower the melting temperature of the molecules containing slow migrating 1(I) and 2(I) chains to 39.5°C (compared to 41.5°C for control), and to delay secretion of the overmodified type I procollagen from OI cells. These data are consistent with a mutation near the carboxyl-terminal end of the triple helical domain which delays triple helical formation and renders all chains available for further post-translational modification amino-terminal to the mutation. Such alterations in triple helical structure, thermal stability, and secretion previously associated only with the lethal OI type II phenotype are thus also seen in the mild OI type IV phenotype. 相似文献
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C Crone J Frokjaer-Jensen JJ Friedman O Christensen 《The Journal of general physiology》1978,71(2):195-220
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Lipoteichoic acid is an important microbe-associated molecular pattern of Lactobacillus rhamnosus GG
Claes Ingmar JJ Segers Marijke E Verhoeven Tine LA Dusselier Michiel Sels Bert F De Keersmaecker Sigrid CJ Vanderleyden Jos Lebeer Sarah 《Microbial cell factories》2012,11(1):1-8
Background
Receptors with a single transmembrane (TM) domain are essential for the signal transduction across the cell membrane. NMR spectroscopy is a powerful tool to study structure of the single TM domain. The expression and purification of a TM domain in Escherichia coli (E.coli) is challenging due to its small molecular weight. Although ketosteroid isomerase (KSI) is a commonly used affinity tag for expression and purification of short peptides, KSI tag needs to be removed with the toxic reagent cyanogen bromide (CNBr).Result
The purification of the TM domain of p75 neurotrophin receptor using a KSI tag with the introduction of a thrombin cleavage site is described herein. The recombinant fusion protein was refolded into micelles and was cleaved with thrombin. Studies showed that purified protein could be used for structural study using NMR spectroscopy.Conclusions
These results provide another strategy for obtaining a single TM domain for structural studies without using toxic chemical digestion or acid to remove the fusion tag. The purified TM domain of p75 neurotrophin receptor will be useful for structural studies. 相似文献10.