MucR from Sinorhizobium meliloti: New Insights into Its DNA Targets and Its Ability to Oligomerize

Author:

Slapakova Martina1,Sgambati Domenico1,Pirone Luciano2ORCID,Russo Veronica1ORCID,D’Abrosca Gianluca3ORCID,Valletta Mariangela1,Russo Rosita1ORCID,Chambery Angela1ORCID,Malgieri Gaetano1ORCID,Pedone Emilia Maria2ORCID,Dame Remus Thei45ORCID,Pedone Paolo Vincenzo1,Baglivo Ilaria1ORCID

Affiliation:

1. Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania “Luigi Vanvitelli”, Via Vivaldi, 43, 81100 Caserta, Italy

2. Institute of Biostructures and Bioimaging, CNR, Via Pietro Castellino, 80134 Naples, Italy

3. Department of Clinical and Experimental Medicine, University of Foggia, Viale Pinto, 1, 71122 Foggia, Italy

4. Leiden Institute of Chemistry, Leiden University, 2333 CC Leiden, The Netherlands

5. Centre for Microbial Cell Biology, Leiden University, 2333 CC Leiden, The Netherlands

Abstract

Proteins of the MucR/Ros family play a crucial role in bacterial infection or symbiosis with eukaryotic hosts. MucR from Sinorhizobium meliloti plays a regulatory role in establishing symbiosis with the host plant, both dependent and independent of Quorum Sensing. Here, we report the first characterization of MucR isolated from Sinorhizobium meliloti by mass spectrometry and demonstrate that this protein forms higher-order oligomers in its native condition of expression by SEC-MALS. We show that MucR purified from Sinorhizobium meliloti can bind DNA and recognize the region upstream of the ndvA gene in EMSA, revealing that this gene is a direct target of MucR. Although MucR DNA binding activity was already described, a detailed characterization of Sinorhizobium meliloti DNA targets has never been reported. We, thus, analyze sequences recognized by MucR in the rem gene promoter, showing that this protein recognizes AT-rich sequences and does not require a consensus sequence to bind DNA. Furthermore, we investigate the dependence of MucR DNA binding on the length of DNA targets. Taken together, our studies establish MucR from Sinorhizobium meliloti as a member of a new family of Histone-like Nucleoid Structuring (H-NS) proteins, thus explaining the multifaceted role of this protein in many species of alpha-proteobacteria.

Publisher

MDPI AG

Subject

Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Computer Science Applications,Spectroscopy,Molecular Biology,General Medicine,Catalysis

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