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新金色分枝杆菌中铁转运成分(分枝杆菌素、外螯合铁素和包膜蛋白)的协调表达

Co-ordinated expression of the components of iron transport (mycobactin, exochelin and envelope proteins) in Mycobacterium neoaurum.

作者信息

Sritharan M, Ratledge C

机构信息

Department of Applied Biology, University of Hull, U.K.

出版信息

FEMS Microbiol Lett. 1989 Jul 15;51(1):183-5. doi: 10.1016/0378-1097(89)90505-3.

Abstract

Mycobacterium neoaurum was grown with a range of iron concentrations from 0.01 to 4.0 micrograms/ml. Synthesis of the extracellular siderophore, exochelin, the intracellular iron storage compound, mycobactin and the iron-repressible envelope proteins were co-ordinately expressed. All three components of the iron transport system were synthesized when low amounts of iron (0.01 to 0.2 micrograms/ml) were added to the medium and were repressed when the iron concentration was increased to 0.5 micrograms/ml and above. These results re-inforce the conclusion that the iron-regulated proteins do fulfil an essential function in iron metabolism.

摘要

新金色分枝杆菌在铁浓度范围为0.01至4.0微克/毫升的条件下培养。细胞外铁载体外螯合素、细胞内铁储存化合物分枝杆菌素以及铁抑制性包膜蛋白的合成是协同表达的。当向培养基中添加少量铁(0.01至0.2微克/毫升)时,铁转运系统的所有三个组分都会合成,而当铁浓度增加到0.5微克/毫升及以上时则受到抑制。这些结果进一步强化了铁调节蛋白在铁代谢中确实发挥重要作用这一结论。

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