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The role of zinc in the stability of the marginally stable IscU scaffold protein. | LitMetric

The role of zinc in the stability of the marginally stable IscU scaffold protein.

Protein Sci

MRC National Institute for Medical Research, The Ridgeway, London, NW7 1AA, United Kingdom; Department of Biochemistry, Biophysics and General Pathology, Seconda Universita' di Napoli, 80138, Naples, Italy.

Published: September 2014

AI Article Synopsis

  • Understanding protein stability reveals insights into evolution influenced by function and environment, particularly concerning the IscU protein, vital for iron-sulfur cluster biogenesis.
  • Our research shows that zinc affects IscU's stability significantly, depending on how the sample was previously treated, with low ionic strength leading to cold denaturation around -8°C.
  • We found that while zinc can stabilize the IscU structure, adding it back after denaturation may lead to protein aggregation, and slight changes in specific amino acids can offset the absence of others in maintaining the protein's stability.

Article Abstract

Understanding the factors that determine protein stability is interesting because it directly reflects the evolutionary pressure coming from function and environment. Here, we have combined experimental and computational methods to study the stability of IscU, a bacterial scaffold protein highly conserved in most organisms and an essential component of the iron-sulfur cluster biogenesis pathway. We demonstrate that the effect of zinc and its consequence strongly depend on the sample history. IscU is a marginally stable protein at low ionic strength to the point that undergoes cold denaturation at around -8°C with a corresponding dramatic decrease of enthalpy, which is consistent with the fluxional nature of the protein. Presence of constitutively bound zinc appreciably stabilizes the IscU fold, whereas it may cause protein aggregation when zinc is added back posthumously. We discuss how zinc coordination can be achieved by different side chains spatially available and all competent for tetrahedral coordination. The individual absence of some of these residues can be largely compensated by small local rearrangements of the others. We discuss the potential importance of our findings in vitro for the function in vivo of the protein.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4243993PMC
http://dx.doi.org/10.1002/pro.2501DOI Listing

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