Structural insight of the full-length Ros protein: a prototype of the prokaryotic zinc-finger family

G D'Abrosca, A Paladino, I Baglivo, L Russo… - Scientific Reports, 2020 - nature.com
Ros/MucR is a widespread family of bacterial zinc-finger (ZF) containing proteins that
integrate multiple functions such as virulence, symbiosis and/or cell cycle transcription. NMR …

The structural role of the zinc ion can be dispensable in prokaryotic zinc-finger domains

I Baglivo, L Russo, S Esposito… - Proceedings of the …, 2009 - National Acad Sciences
The recent characterization of the prokaryotic Cys2His2 zinc-finger domain, identified in Ros
protein from Agrobacterium tumefaciens, has demonstrated that, although possessing a …

The Ros/MucR zinc-finger protein family in bacteria: structure and functions

M Janczarek - International Journal of Molecular Sciences, 2022 - mdpi.com
Ros/MucR is a widespread family of bacterial zinc-finger-containing proteins that integrate
multiple functions, such as symbiosis, virulence, transcription regulation, motility, production …

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

G Malgieri, M Palmieri, L Russo, R Fattorusso… - The FEBS …, 2015 - Wiley Online Library
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 …

Copper (I) or (II) Replacement of the Structural Zinc Ion in the Prokaryotic Zinc Finger Ros Does Not Result in a Functional Domain

M Dragone, R Grazioso, G D'Abrosca, I Baglivo… - International Journal of …, 2022 - mdpi.com
A strict interplay is known to involve copper and zinc in many cellular processes. For this
reason, the results of copper's interaction with zinc binding proteins are of great interest. For …

An Experimentally Tested Scenario for the Structural Evolution of Eukaryotic Cys2His2 Zinc Fingers from Eubacterial Ros Homologs

F Netti, G Malgieri, S Esposito… - Molecular biology …, 2013 - academic.oup.com
The exact evolutionary origin of the zinc finger (ZF) domain is unknown, as it is still not clear
from which organisms it was first derived. However, the unique features of the ZF domains …

The prokaryotic Cys2His2 zinc-finger adopts a novel fold as revealed by the NMR structure of Agrobacterium tumefaciens Ros DNA-binding domain

G Malgieri, L Russo, S Esposito… - Proceedings of the …, 2007 - National Acad Sciences
The first putative prokaryotic Cys2His2 zinc-finger domain has been identified in the
transcriptional regulator Ros from Agrobacterium tumefaciens, indicating that the Cys2His2 …

Molecular strategies to replace the structural metal site in the prokaryotic zinc finger domain

I Baglivo, M Palmieri, A Rivellino, F Netti… - … et Biophysica Acta (BBA …, 2014 - Elsevier
The specific arrangement of secondary elements in a local motif often totally relies on the
formation of coordination bonds between metal ions and protein ligands. This is typified by …

A Novel Type of Zinc Finger DNA Binding Domain in the Agrobacterium tumefaciens Transcriptional Regulator Ros

S Esposito, I Baglivo, G Malgieri, L Russo… - Biochemistry, 2006 - ACS Publications
Transcriptional factors bearing a Cys2His2 zinc finger were thought to be confined to
eukaryotes, but recent studies have suggested their presence also in prokaryotes. In this …

[HTML][HTML] Ancestral zinc-finger bearing protein MucR in alpha-proteobacteria: a novel xenogeneic silencer?

J Jiao, CF Tian - Computational and Structural Biotechnology Journal, 2020 - Elsevier
Abstract The MucR/Ros family protein is conserved in alpha-proteobacteria and
characterized by its zinc-finger motif that has been proposed as the ancestral domain from …