ArticleScientific reports2017
Ml proteins from Mesorhizobium loti and MucR from Brucella abortus: an AT-rich core DNA-target site and oligomerization ability.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Identifying Two New Ros/MucR Proteins: An Atypical Structure with a Divergent Function.Biomolecules · 2026Article
- Rok from B. subtilis: Bridging genome structure and transcription regulation.Molecular microbiology · 2025Review
- Circular oligomeric particles formed by Ros/MucR family members mediate DNA organization in α-proteobacteria.Nucleic acids research · 2024Article
- MucR fromInternational journal of molecular sciences · 2023Article
- The Ros/MucR Zinc-Finger Protein Family in Bacteria: Structure and Functions.International journal of molecular sciences · 2022Review
- Copper (I) or (II) Replacement of the Structural Zinc Ion in the Prokaryotic Zinc Finger Ros Does Not Result in a Functional Domain.International journal of molecular sciences · 2022Article
- The convergent xenogeneic silencer MucR predisposes α-proteobacteria to integrate AT-rich symbiosis genes.Nucleic acids research · 2022Article
- Structural Insight of the Full-Length Ros Protein: A Prototype of the Prokaryotic Zinc-Finger Family.Scientific reports · 2020Article
- Different Impacts of MucR Binding to theBiomolecules · 2020Article
- Ancestral zinc-finger bearing protein MucR in alpha-proteobacteria: A novel xenogeneic silencer?Computational and structural biotechnology journal · 2020Review
- Identifying the region responsible for Brucella abortus MucR higher-order oligomer formation and examining its role in gene regulation.Scientific reports · 2018Article
- MucR binds multiple target sites in the promoter of its own gene and is a heat-stable protein: Is MucR a H-NS-like protein?FEBS open bio · 2018Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mesorhizobium loti contains ten genes coding for proteins sharing high amino acid sequence identity with members of the Ros/MucR transcription factor family. Five of these Ros/MucR family members from Mesorhizobium loti (Ml proteins) have been recently structurally and functionally characterized demonstrating that Ml proteins are DNA-binding proteins. However, the DNA-binding studies were performed using the Ros DNA-binding site with the Ml proteins. Currently, there is no evidence as to when the Ml proteins are expressed during the Mesorhizobium lo ti life cycle as well as no information concerning their natural DNA-binding site. In this study, we examine the ml genes expression profile in Mesorhizobium loti and show that ml1, ml2, ml3 and ml5 are expressed during planktonic growth and in biofilms. DNA-binding experiments show that the Ml proteins studied bind a conserved AT-rich site in the promoter region of the exoY gene from Mesorhizobium loti and that the proteins make important contacts with the minor groove of DNA. Moreover, we demonstrate that the Ml proteins studied form higher-order oligomers through their N-terminal region and that the same AT-rich site is recognized by MucR from Brucella abortus using a similar mechanism involving contacts with the minor groove of DNA and oligomerization.
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