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J Biol Inorg Chem. 2011 Oct;16(7):1011-24. doi: 10.1007/s00775-011-0790-y. Epub 2011 May 19.

Bacterial metallothioneins: past, present, and questions for the future.

Author information

1
Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK. c.blindauer@warwick.ac.uk

Abstract

Bacterial metallothioneins (MTs) have been known since the mid-1980s. The only family known until recently was the BmtA family, exemplified by the zinc- and cadmium-binding SmtA from the cyanobacterium Synechococcus PCC 7942, for which a structure was determined in 2001. Only in 2008 was a second type of bacterial MT identified in mycobacteria, and the copper-binding gene product was called MymT. Many of the features of SmtA either have been unexpected or are otherwise "unusual", for example the presence of a zinc finger fold and the kinetic inertness of one of the four zinc ions bound to the protein. The unpredictability of molecular properties of this protein exemplified the need for continued biophysical studies of novel proteins. Homologues for SmtA have been identified in a limited number of bacterial genomes from cyanobacteria, pseudomonads, alphaproteobacteria, gammaproteobacteria, and firmicutes. Except for the residues defining the zinc finger fold, these homologous protein sequences display an intriguing variety, especially in terms of metal ligand position and identity. The increased number of homologues has allowed use of hidden Markov models to look for more remote relatives of SmtA, leading to the identification of a novel family of putative hybrid LIM domain MTs. However, database searches based on sequence similarity are of limited use for mining for further "overlooked" bacterial MTs, as so far undiscovered bacterial MTs may be too diverse from any other known MTs, and other approaches are required.

PMID:
21594652
DOI:
10.1007/s00775-011-0790-y
[Indexed for MEDLINE]

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