title: The prokaryotic zinc-finger: structure, function and comparison with the eukaryotic counterpart.
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.
authors.affiliation: Department of Environmental, Biological and Pharmaceutical Science and Technology, II University of Naples, Caserta, Italy.
authors.forename: Gaetano
authors.initials: G
authors.lastname: Malgieri
authors.affiliation: Department of Environmental, Biological and Pharmaceutical Science and Technology, II University of Naples, Caserta, Italy.
authors.forename: Maddalena
authors.initials: M
authors.lastname: Palmieri
authors.affiliation: Department of Environmental, Biological and Pharmaceutical Science and Technology, II University of Naples, Caserta, Italy.
authors.forename: Luigi
authors.initials: L
authors.lastname: Russo
authors.affiliation: Department of Environmental, Biological and Pharmaceutical Science and Technology, II University of Naples, Caserta, Italy.|Interuniversity Research Centre on Bioactive Peptides, University of Naples 'Federico II', Naples, Italy.
authors.forename: Roberto
authors.initials: R
authors.lastname: Fattorusso
authors.affiliation: Department of Environmental, Biological and Pharmaceutical Science and Technology, II University of Naples, Caserta, Italy.|Interuniversity Research Centre on Bioactive Peptides, University of Naples 'Federico II', Naples, Italy.
authors.forename: Paolo V
authors.initials: PV
authors.lastname: Pedone
authors.affiliation: Department of Environmental, Biological and Pharmaceutical Science and Technology, II University of Naples, Caserta, Italy.|Interuniversity Research Centre on Bioactive Peptides, University of Naples 'Federico II', Naples, Italy.
authors.forename: Carla
authors.initials: C
authors.lastname: Isernia
mesh_terms: D016960:Agrobacterium tumefaciens / Q000378:metabolism; D005057:Eukaryotic Cells / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D011387:Prokaryotic Cells / Q000737:chemistry / Q000378:metabolism*; D016335:Zinc Fingers
keywords: DNA binding; cadmium; evolution; folding pathway; zinc finger