作者: Igor Stojiljkovic , Klaus Hantke
DOI: 10.1007/BF00705650
关键词:
摘要: The functions of N- and C-terminal domains the Fur repressor ofEscherichia coli in promoter recognition dimerization were studied. We investigated ability fusion proteins containing or domain to dimerize repress a Fur-regulatedlacZ gene. N-terminal domain, when fused C1857, repressed fusion. However, Fur-CI857 was unable complement growth defect anE. fur mutant on fumarate succinate. Fur, N-terminus CI857, λP, -regulatedlacZ fusion, indicating chimeric protein, which is prerequisite for Cl activity. Both fully active under both iron-rich iron-poor conditions. conclude that involved Fur-responsive C-terminus mediates oligomerization repressor.