Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.64 (proteinase K)
 4,071 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A recently described protein, metaxin 1, serves as a component of a preprotein import complex in the outer membrane of the mammalian mitochondrion. A yeast two-hybrid screen with metaxin 1 as bait has now identified a novel protein, which we have termed metaxin 2, as a metaxin 1-binding protein. Metaxin 2 shares 29% identity with metaxin 1 at the amino acid level, but metaxin 2, unlike metaxin 1, lacks a C-terminal mitochondrial outer membrane signal-anchor domain. Two C. elegans hypothetical proteins, CelZC97.1 and CelF39B2.i, share high sequence similarity with metaxin 2 and metaxin 1, respectively, and likely represent the C. elegans orthologs. Affinity-purified antibodies against metaxin 2 were prepared against the recombinant protein produced in E. coli and were used to analyze the subcellular distribution of metaxin 2. In subcellular fractions of mouse liver, a 29 kD immunoreactive protein, consistent in size with the predicted translation product of metaxin 2 cDNA, was found solely in mitochondria. Alkali extraction of mitochondria indicated that metaxin 2 is peripherally associated with mitochondrial membranes. Metaxin 2 in intact mitochondria was susceptible to digestion with proteinase K, indicating that metaxin 2 is located on the cytosolic face of the mitochondrial outer membrane. Finally, baculoviruses encoding a His6-tagged metaxin 2 and an untagged metaxin 1 lacking its C-terminal transmembrane domain were produced and used separately or in combination to infect Sf21 insect cells. Metaxin 1 bound to a Ni2+-chelate affinity column only in the presence of metaxin 2, indicating that metaxin 1 and metaxin 2 interact when overexpressed in insect cells. These results suggest that metaxin 2 is bound to the cytosolic face of the mitochondrial outer membrane by means of its interaction with membrane-bound metaxin 1, and that this complex may play a role in protein import into mammalian mitochondria.
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PMID:Metaxin 1 interacts with metaxin 2, a novel related protein associated with the mammalian mitochondrial outer membrane. 1038 Dec 57

Adhesion and colonisation properties of three probiotic strains namely, Lactobacillus rhamnosus DR20, L. acidophilus HN017, and Bifidobacterium lactis DR10, were determined in vitro using the differentiated human intestinal cell-lines including HT-29, Caco-2, and HT29-MTX, and compared with properties of L. acidophilus LA-1 and L. rhamnosus GG (two commercial probiotic strains). Two independent methods were employed to quantitate the "adhesiveness" of each strain. In the first method, the bacteria adhered to human cells were detected by Gram staining and counted in different fields under a microscope. Bacteria were also radio-labelled and extent of adhesion determined by scintillation counting. All three strains showed strong adhesion with the human intestinal cell lines in vitro. Adhesion indices of the three strains to two cell lines, i.e. HT-29, and Caco-2 varied between 99 +/- 17 and 219 +/- 36. With mucus-secreting cell-line HT29-MTX, the adhesion indices of all the strains were 2-3 times higher. The adhesion indices of L. acidophilus LA-1 and L. rhamnosus GG were comparable to the other three probiotic strains. We also investigated the inhibitory effect of adhering strains against the intestinal cell monolayer colonization by a known enterotoxigenic strain of Escherichia coli (strain O157:H7). Pre-treatment of E. coli O157:H7 with 2.5-fold concentrated cell-free culture supernatants from L. acidophilus HN017, L. rhamnosus DR20 and B. lactis DR10 reduced the culturable E. coli numbers on TSB plates and also reduced the invasiveness and cell association characteristics of this toxic strain. The inhibitory molecules secreted into the spent media by these strains were partially affected by treatments with lactate dehydrogenase, trypsin and proteinase K suggesting that overall inhibition may be due to a synergistic action of lactic acid and proteinaceous substances.
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PMID:In vitro adherence properties of Lactobacillus rhamnosus DR20 and Bifidobacterium lactis DR10 strains and their antagonistic activity against an enterotoxigenic Escherichia coli. 1151 30