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The prokaryotic zinc‐finger: structure, function and comparison with the eukaryotic counterpart
Author(s) -
Malgieri Gaetano,
Palmieri Maddalena,
Russo Luigi,
Fattorusso Roberto,
Pedone Paolo V.,
Isernia Carla
Publication year - 2015
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13503
Subject(s) - zinc finger , eukaryotic cell , computational biology , function (biology) , biology , regulator , domain (mathematical analysis) , genetics , microbiology and biotechnology , gene , transcription factor , mathematical analysis , mathematics
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 Cys 2 His 2 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 ZF s, summarizing and discussing differences and analogies with the eukaryotic domains and providing important insights into their structure/function relationships.