The prokaryotic zinc-finger: structure, function and comparison with the eukaryotic counterpart

Gaetano Malgieri; Maddalena Palmieri; Luigi Russo; Roberto Fattorusso; Paolo V Pedone; Carla Isernia

doi:10.1111/febs.13503

The prokaryotic zinc-finger: structure, function and comparison with the eukaryotic counterpart

FEBS J. 2015 Dec;282(23):4480-96. doi: 10.1111/febs.13503. Epub 2015 Oct 6.

Authors

Gaetano Malgieri¹, Maddalena Palmieri¹, Luigi Russo¹, Roberto Fattorusso^{1

2}, Paolo V Pedone^{1

2}, Carla Isernia^{1

2}

Affiliations

¹ Department of Environmental, Biological and Pharmaceutical Science and Technology, II University of Naples, Caserta, Italy.
² Interuniversity Research Centre on Bioactive Peptides, University of Naples 'Federico II', Naples, Italy.

PMID: 26365095
DOI: 10.1111/febs.13503

Abstract

Classical zinc finger (ZF) domains were thought to be confined to the eukaryotic kingdom until the transcriptional regulator Ros protein was identified in Agrobacterium tumefaciens. The Ros Cys2 His2 ZF binds DNA in a peculiar mode and folds in a domain significantly larger than its eukaryotic counterpart consisting of 58 amino acids (the 9-66 region) arranged in a βββαα topology, and stabilized by a conserved, extensive, 15-residue hydrophobic core. The prokaryotic ZF domain, then, shows some intriguing new features that make it interestingly different from its eukaryotic counterpart. This review will focus on the prokaryotic ZFs, summarizing and discussing differences and analogies with the eukaryotic domains and providing important insights into their structure/function relationships.

Keywords: DNA binding; cadmium; evolution; folding pathway; zinc finger.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't
Review

MeSH terms

Agrobacterium tumefaciens / metabolism
Eukaryotic Cells / chemistry
Eukaryotic Cells / metabolism*
Humans
Prokaryotic Cells / chemistry
Prokaryotic Cells / metabolism*
Zinc Fingers*