AI Article Synopsis

  • The study investigates the dimerization properties of H-NS family proteins TurA and TurB from Pseudomonas putida KT2440 and Pmr from the pCAR1 plasmid.
  • Chemical cross-linking analyses reveal that TurA and TurB show a stronger affinity for forming dimers with each other than with Pmr.
  • Additionally, truncated TurB showed a higher tendency to form oligomers with itself and TurA, further indicating that TurA and TurB interact more robustly than with Pmr.

Article Abstract

H-NS family proteins encoded on the chromosome of Pseudomonas putida KT2440 (TurA and TurB) and the IncP-7 plasmid pCAR1 (Pmr) commonly have an N-terminal dimerization/oligomerization domain constituted by a central and a terminal dimerization sites. To clarify the dimerization manner at the central dimerization sites of the three homologs, we performed chemical cross-linking analyses with protein variants inactivated at the terminal dimerization site. Comparison of the hetero-dimer ratios among them suggested stronger affinities between the central dimerization sites of TurA and TurB monomers than between TurA and Pmr or TurB and Pmr. Furthermore, analyses of the interaction between truncated TurB containing only a functional terminal dimerization site and full-length proteins suggested that TurB exhibited higher affinities for oligomer complex formation with TurB itself and TurA but not Pmr. Altogether, we revealed stronger interaction between the N-terminal domains of TurA and TurB than between either of them and Pmr.

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http://dx.doi.org/10.1080/09168451.2018.1484277DOI Listing

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H-NS family proteins regulate the expression of many genes by preferably binding to AT-rich genomic regions and altering DNA topology. They are found in both bacterial chromosomes and plasmids, and plasmid-encoded H-NS family proteins have sometimes been suggested to act as a molecular backup of the chromosomally encoded ones. Pmr is an H-NS family protein encoded on the catabolic plasmid pCAR1, which belongs to incompatibility P-7 group.

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Article Synopsis
  • The study investigates the dimerization properties of H-NS family proteins TurA and TurB from Pseudomonas putida KT2440 and Pmr from the pCAR1 plasmid.
  • Chemical cross-linking analyses reveal that TurA and TurB show a stronger affinity for forming dimers with each other than with Pmr.
  • Additionally, truncated TurB showed a higher tendency to form oligomers with itself and TurA, further indicating that TurA and TurB interact more robustly than with Pmr.
View Article and Find Full Text PDF

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MvaT proteins are members of the H-NS family of proteins in pseudomonads. The IncP-7 conjugative plasmid pCAR1 carries an mvaT-homologous gene, pmr. In Pseudomonas putida KT2440 bearing pCAR1, pmr and the chromosomally carried homologous genes, turA and turB, are transcribed at high levels, and Pmr interacts with TurA and TurB in vitro.

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