Brown J A, Glenn J K, Gold M H
Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton 97006-1999.
J Bacteriol. 1990 Jun;172(6):3125-30. doi: 10.1128/jb.172.6.3125-3130.1990.
The appearance of manganese peroxidase (MnP) activity in nitrogen-limited cultures of Phanerochaete chrysosporium is dependent on the presence of manganese. Cultures grown in the absence of Mn developed normally and produced normal levels of the secondary metabolite veratryl alcohol but produced no MnP activity. Immunoblot analysis indicated that appearance of MnP protein in the extracellular medium was also dependent on the presence of Mn. Intracellular MnP protein was detectable only in cells grown in the presence of Mn. MnP mRNA was detected by Northern (RNA) blot analysis only in cells grown in the presence of Mn. If Mn was added to 4-day-old nitrogen-limited Mn-deficient cultures, extracellular MnP activity appeared after 6 h and reached a maximum after 18 h. Both actinomycin D and cycloheximide inhibited the induction of MnP activity by Mn. These results indicate that Mn, the substrate of the enzyme, is involved in the transcriptional regulation of the MnP gene.
在氮限制条件下培养的黄孢原毛平革菌中，锰过氧化物酶（MnP）活性的出现依赖于锰的存在。在无锰条件下生长的培养物正常发育，并产生正常水平的次生代谢产物藜芦醇，但不产生MnP活性。免疫印迹分析表明，细胞外培养基中MnP蛋白的出现也依赖于锰的存在。仅在有锰存在的情况下生长的细胞中可检测到细胞内MnP蛋白。通过Northern（RNA）印迹分析仅在有锰存在的情况下生长的细胞中检测到MnP mRNA。如果将锰添加到4日龄的氮限制缺锰培养物中，6小时后出现细胞外MnP活性，18小时后达到最大值。放线菌素D和环己酰亚胺均抑制锰对MnP活性的诱导。这些结果表明，该酶的底物锰参与了MnP基因的转录调控。
