Accumulation of Uridinediphospho-N-acetylmuramyl-peptides Induced by Glycine and Penicillin |
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Authors: | Fumio Hishinuma Tsutomu Naito Kazuo Izaki Hajime Takahashi |
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Institution: | Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Sendai 980 |
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Abstract: | The genes POX2 and POX4, which encode the subunits (PXP-2 and PXP-4) of peroxisomal fatty acyl-coenzyme A oxidase of Candida tropicalis, were introduced into the related yeast Candida maltosa. The cells transformed with POX2 or POX4 gave much PXP-2 or PXP-4 in the purified peroxisomes. The polypeptides associated with the heterologous organelle were resistant to added protease, implying that they were transported into the peroxisomes. Genes for curtailed versions of PXP-4 were constructed in vitro and introduced into the host cells. Peptide-C, the COOH-terminal two-thirds of PXP-4, was efficiently transported into the host peroxisomes, and the polypeptide containing the NH2-terminal one-third was also, in much lesser amount. These and other results suggested that there were at least two regions of peroxisomal targeting information in PXP-4 and the primary information was internal. The deletions in Peptide-C inhibited the transport of many, but not all, of the host-cell peroxisomal polypeptides. This suggested heterogeneous transport systems on the peroxisomal membrane. |
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Keywords: | bacteriocin Lactobacillus acidophilus lactic acid bacteria micro-plate |
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