Interactions of toxic metals with fungi have long been of importance since metal toxicity still is the basis of many fungicidal preparations while in an environmental context, accelerating pollution of the natural environment has led to increased interest because of the sometimes dominant presence of fungi in metal-polluted habitats, the translocation of toxic metals and radionuclides to fruit bodies of edible higher fungi, and the significance of mycorrhizal fungi in the amelioration of metal phytotoxicity (Colpaert and Van Assche, 1987). Furthermore, the use of fungal (and other microbial) biomass for the detoxification of metal/radionuclide-containing industrial effluents is of biotechnological potential (Gadd, 1990, 1992a).

Interactions of fungip with toxic metals

https://www.cell.com/trends/biotechnology/pdf/S0167-7799(00)01534-1.pdf

Metal-binding proteins and peptides in bioremediation and phytoremediation of heavy metals

https://www.cell.com/trends/biotechnology/pdf/0167-7799(93)90158-6.pdf

Microbial treatment of metal pollution — a working biotechnology?

Recent concerns on the radiotoxicity and longevity of nuclides have prompted the development of new technologies for their removal from wastes produced from nuclear power programs and nuclear fuel reprocessing activities. Alongside developments from traditional chemical treatment processes, interest has also centered on the application of biotechnology for efficient waste treatment. Many biological techniques have relied on empirical approaches in simple model systems, with scant regard to the nature and volume of actual target wastes; such considerations may limit the application of the new technologies in practice. This review aims to identify some of the likely problems, to discuss the various approaches under current consideration, and to evaluate ways in which either the target waste or the detoxifying biomass may be modified or presented for the most efficient treatment.

The application of biotechnology to the treatment of wastes produced from the nuclear fuel cycle: biodegradation and bioaccumulation as a means of treating radionuclide-containing streams.

Yeast (CUP1) and mammalian (HMT-1A) metallothioneins (MTs) have been efficiently expressed in Escherichia coli as fusions to the outer membrane protein LamB. A 65-amino-acid sequence from the CUP1 protein of Saccharomyces cerevisiae (yeast [Y] MT) was genetically inserted in permissive site 153 of the LamB sequence, which faces the outer medium. A second LamB fusion at position 153 was created with 66 amino acids recruited from the form of human (H) MT that is predominant in the adipose tissue, HMT-1A. Both LamB153-YMT and LamB153-HMT hybrids were produced in vivo as full-length proteins, without any indication of instability or proteolytic degradation. Each of the two fusion proteins was functional as the port of entry of lambda phage variants, suggesting maintenance of the overall topology of the wild-type LamB. Expression of the hybrid proteins in vivo multiplied the natural ability of E. coli cells to bind Cd2+ 15- to 20-fold, in good correlation with the number of metal-binding centers contributed by the MT moiety of the fusions.

Metalloadsorption by Escherichia coli cells displaying yeast and mammalian metallothioneins anchored to the outer membrane protein LamB.

The yeast metallothionein gene CUP1 was cloned into a bacterial expression system to achieve efficient, controlled expression of the stable, unprocessed protein product. The Escherichia coli-synthesized yeast metallothionein bound copper, cadmium, and zinc, indicating that the protein was functional. Furthermore, E. coli cells expressing CUP1 acquired a new, inducible ability to selectively sequester heavy metal ions from the growth medium.

J Zimmerman

Papers

Efficient expression of the yeast metallothionein gene in Escherichia coli.