Identification of a 29 kDa protein in the envelope of Mycobacterium smegmatis as a putative ferri-exochelin receptor

Article Abstract:

The 29 kDa iron-regulated protein in the envelope of Mycobacterium smegmatis is a ferri-exochelin receptor. The protein forms a complex with 55Fe(III)-exochelin in an envelope preparation from cells lacking iron. The non-denaturing detergent CHAPS efficiently extracts the complex. Affinity chromatography of the complex using a ferri-exochelin-Sepharose 4B matrix results in retention of a 29 kDa and a 25 kDa protein. The 25 kDa protein probably functions in the formation and maintenance of the ferri-exochelin receptor.

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The occurrence of carboxymycobactin, the siderophore of pathogenic mycobacteria, as a second extracellular siderophore in Mycobacterium smegmatis

Article Abstract:

Culture filtrates of the non-pathogen Mycobacterium smegmatis showed the occurrence of a carboxymycobactin as a second extracellular siderophore. As many as 12 similar molecules were produced, with various chain lengths that can be detected by HPLC or HPTLC. Its presence indicates a wider spread of the molecule than previously thought, despite its being a minor siderophore component as evidenced by the amount generated by M. smegmatis.

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Polyadenylylation in mycobacteria: evidence for oligo(dT)-primed cDNA synthesis

Article Abstract:

Polyadenylylation of mRNA appears to be common in the mycobacteria. RNA polyadenylylation controls plasmid replication, modulates RNA stability and may participate in mRNA translation.

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