✍ Scribed by Andre Schmidt; Matthias Hagen; Eileen Schütze; Astrid Schmidt; Prof. Dr. Erika Kothe
No coin nor oath required. For personal study only.
Metallothioneins and metallohistins are short peptides with a high cysteine and/or histidine content able to coordinate metals intracellularly, thereby increasing the tolerance against elevated concentrations of metals. Because of their features, they can be detected by in silico prediction from proteomes annotated from sequenced genomes. Here, we analyzed 73 sequenced actinobacterial genomes for peptides (≤100 amino acids) with a high content of cysteine and histidine (≥15%) and identified 103 putative metallothioneins and metallohistins. For 45 of these peptides, we found similarities to metal binding protein domains, including zinc fingers, heavy metal transporters or eukaryotic metallothioneins, which can serve as proof‐of‐principle in underscoring a potential function as metal binding peptides. An evolutionary origin from metal containing domains of enzymes is discussed and metallohistins not containing cysteine are described for the first time for bacteria. (© 2010 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)
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