Picture of sea vessel plough through rough maritime conditions

Innovations in marine technology, pioneered through Open Access research...

Strathprints makes available scholarly Open Access content by researchers in the Department of Naval Architecture, Ocean & Marine Engineering based within the Faculty of Engineering.

Research here explores the potential of marine renewables, such as offshore wind, current and wave energy devices to promote the delivery of diverse energy sources. Expertise in offshore hydrodynamics in offshore structures also informs innovations within the oil and gas industries. But as a world-leading centre of marine technology, the Department is recognised as the leading authority in all areas related to maritime safety, such as resilience engineering, collision avoidance and risk-based ship design. Techniques to support sustainability vessel life cycle management is a key research focus.

Explore the Open Access research of the Department of Naval Architecture, Ocean & Marine Engineering. Or explore all of Strathclyde's Open Access research...

A metallothionein containing a zinc finger within a four-metal cluster protects a bacterium from zinc toxicity

Parkinson, J.A. and Blindauer, C.A. and Harrison, M.D. and Robinson, A.K. and Turner-Cavfet, J.S. and Robinson, N.J. and Sadler, P.J. (2001) A metallothionein containing a zinc finger within a four-metal cluster protects a bacterium from zinc toxicity. Proceedings of the National Academy of Sciences, 98 (17). pp. 9593-9598. ISSN 1091-6490

Full text not available in this repository. Request a copy from the Strathclyde author

Abstract

Zinc is essential for many cellular processes, including DNA synthesis, transcription, and translation, but excess can be toxic. A zinc-induced gene, smtA, is required for normal zinc-tolerance in the cyanobacterium Synechococcus PCC 7942. Here we report that the protein SmtA contains a cleft lined with Cys-sulfur and His-imidazole ligands that binds four zinc ions in a Zn4Cys9His2 cluster. The thiolate sulfurs of five Cys ligands provide bridges between the two ZnCys4 and two ZnCys3His sites, giving two fused six-membered rings with distorted boat conformations. The inorganic core strongly resembles the Zn4Cys11 cluster of mammalian metallothionein, despite different amino acid sequences, a different linear order of the ligands, and presence of histidine ligands. Also, SmtA contains elements of secondary structure not found in metallothioneins. One of the two Cys4-coordinated zinc ions in SmtA readily exchanges with exogenous metal (111Cd), whereas the other is inert. The thiolate sulfur ligands bound to zinc in this site are buried within the protein. Regions of β-strand and α-helix surround the inert site to form a zinc finger resembling the zinc fingers in GATA and LIM-domain proteins. Eukaryotic zinc fingers interact specifically with other proteins or DNA and an analogous interaction can therefore be anticipated for prokaryotic zinc fingers. SmtA now provides structural proof for the existence of zinc fingers in prokaryotes, and sequences related to the zinc finger motif can be identified in several bacterial genomes.