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

Scientific Reports
Gianluca D'AbroscaGaetano Malgieri

Abstract

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.

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Citations

Dec 12, 2020·Computational and Structural Biotechnology Journal·Jian Jiao, Chang-Fu Tian
Dec 5, 2020·Scientific Reports·Rinaldo GraziosoGaetano Malgieri

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Methods Mentioned

BETA
Nuclear Magnetic Resonance
NMR
PCR
size-exclusion chromatography
light scattering

Software Mentioned

Maestro
Rosetta
CARA
Gromacs
Jpred
TOPSPIN
Astra

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