Extensive deproteinization of Dictyostelium discoideum RNase P reveals a new catalytic activity.
Nuclear Dictyostelium discoideum RNase P was subjected to vigorous deproteinization procedures. After treatment with proteinase K followed by phenol extraction of samples containing D. discoideum RNase P activity, a new enzymatic activity was recovered. The proteinase K/phenol/SDS treated enzyme cleaves Schizossacharomyces pombe tRNAser (supS1), D. discoideum tRNASer and tRNALeu precursors several nucleotides upstream of the cleavage site of RNase P, liberating products with 5'-hydroxyl ends. This activity seems to be associated with one or two RNA molecules copurifying with D. discoideum RNase P activity as judged by its inhibition in the presence of micrococcal nuclease, which is in contrast to its resistance to proteinase K/phenol/SDS treatment.
Department of Biochemistry, School of Medicine, University of Patras, Patras, Greece.
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Stathopoulos
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Zarkadis
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Drainas
D000818:Animals; D001483:Base Sequence; D002384:Catalysis; D004023:Dictyostelium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D019286:Endopeptidase K / Q000378:metabolism; D004722:Endoribonucleases / Q000737:chemistry*; D008836:Micrococcal Nuclease / Q000378:metabolism; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010636:Phenols; D012322:RNA Precursors / Q000378:metabolism; D016337:RNA, Catalytic / Q000737:chemistry*; D012362:RNA, Transfer, Ser / Q000378:metabolism; D043262:Ribonuclease P; D013329:Structure-Activity Relationship
D010636:Phenols; D012322:RNA Precursors; D016337:RNA, Catalytic; D012362:RNA, Transfer, Ser; D004722:Endoribonucleases; D043262:Ribonuclease P; D008836:Micrococcal Nuclease; D019286:Endopeptidase K