Heterologous Expression of Full-Length and Truncated Human ZIP4 Zinc Transporter in Saccharomyces cerevisiae

Biomolecules. 2022 May 21;12(5):726. doi: 10.3390/biom12050726.

Abstract

The human (h) transporter hZIP4 is the primary Zn2+ importer in the intestine. hZIP4 is also expressed in a variety of organs such as the pancreas and brain. Dysfunction of hZIP4 can result in the Zn2+ deficiency disease acrodermatitis enteropathica (AE). AE can disrupt digestive and immune system homeostasis. A limited number of hZIP4 expression strategies have hindered increasing knowledge about this essential transmembrane protein. Here, we report the heterologous expression of hZIP4 in Saccharomyces cerevisiae. Both a wild-type and a mutant S. cerevisiae strain, in which the endogenous Zn2+ transporters were deleted, were used to test the expression and localization of an hZIP4-GFP fusion protein. A full-length hZIP4-GFP and a truncated membrane-domain-only (mhZIP4-GFP) protein were observed to be present in the plasma membrane in yeast.

Keywords: GFP fusion protein; heterologous expression in yeast; human zinc transporter; membrane protein.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Acrodermatitis* / metabolism
  • Carrier Proteins
  • Cation Transport Proteins* / genetics
  • Cation Transport Proteins* / metabolism
  • Humans
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Zinc / deficiency

Substances

  • Carrier Proteins
  • Cation Transport Proteins
  • zinc-binding protein
  • Zinc

Supplementary concepts

  • Acrodermatitis enteropathica