Structural Insight of the Full-Length Ros Protein: A Prototype of the Prokaryotic Zinc-Finger Family

Structural Insight of the Full-Length Ros Protein: A Prototype of the Prokaryotic Zinc-Finger Family (68 views visite)

D'Abrosca G, Paladino A, Baglivo I, Russo L, Sassano M, Grazioso R, Iacovino R, Pirone L, Pedone E, Pedone P, Isernia C, Fattorusso R, Malgieri G

Sci Rep (ISSN: 2045-2322, 2045-2322linking), 2020 Jun 9; 10(1): 9283-9283.

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Paper type Tipo di articolo: Journal Article, Paper, Research Support, Non-U. S. Gov'T

Impact factor: 4.011, 5-year impact factor Impact factor a 5 anni: 4.525

Url: https://doi.org/10.1038/s41598-020-66204-5

Keywords Parole chiave: Agrobacterium Tumefaciens Genetics Metabolism , Amino Acid Sequence , Bacterial Proteins Genetics Metabolism , Binding Sites , Dna-Binding Proteins Genetics Metabolism , Models, Molecular , Nuclear Magnetic Resonance, Biomolecular , Protein Domains , Protein Structure, Secondary Genetics , Zinc Fingers Genetics

Affiliations Affiliazioni:
*** IBB - CNR ***

Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania “Luigi Vanvitelli”, via Vivaldi, 43, 81100, Caserta, Italy
Gianluca D’Abrosca, Antonella Paladino, Ilaria Baglivo, Luigi Russo, Marica Sassano, Rinaldo Grazioso, Rosa Iacovino, Paolo Vincenzo Pedone, Carla Isernia, Roberto Fattorusso & Gaetano Malgieri
SCITEC-CNR, via Mario Bianco 9, 20131, Milano, Italy
Institute of Biostructures and Bioimaging - CNR, Via Mezzocannone 16, 80134, Naples, Italy
Luciano Pirone & Emilia Maria Pedone

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Structural Insight of the Full-Length Ros Protein: A Prototype of the Prokaryotic Zinc-Finger Family

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 solution structure of Ros DNA-binding domain (region 56–142, i.e. Ros87) has been solved by our group and shows that the prokaryotic ZF domain shows interesting structural and functional features that differentiate it from its eukaryotic counterpart as it folds in a significantly larger zinc-binding globular domain. We have recently proposed a novel functional model for this family of proteins suggesting that they may act as H-NS-‘like’ gene silencers. Indeed, the N-terminal region of this family of proteins appears to be responsible for the formation of functional oligomers. No structural characterization of the Ros N-terminal domain (region 1–55) is available to date, mainly because of serious solubility problems of the full-length protein. Here we report the first structural characterization of the N-terminal domain of the prokaryotic ZF family examining by means of MD and NMR the structural preferences of the full-length Ros protein from Agrobacterium tumefaciens.