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Article

Molecular and Functional Characterization of MobK Protein—A Novel-Type Relaxase Involved in Mobilization for Conjugational Transfer of Klebsiella pneumoniae Plasmid pIGRK

1
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland
2
Department of Biomedical Technology, Cosmetics Chemicals and Electrochemistry, Łukasiewicz Research Network—Industrial Chemistry Institute, Rydygiera 8, 01-793 Warsaw, Poland
3
Central Forensic Laboratory of the Police, Biology Department, Iwicka 14, 00-735 Warsaw, Poland
4
Curiosity Diagnostics Sp. z o.o., Duchnicka 3, Building 16, Entrance A, 01-796 Warsaw, Poland
*
Author to whom correspondence should be addressed.
Academic Editor: Baltasar Mayo
Int. J. Mol. Sci. 2021, 22(10), 5152; https://doi.org/10.3390/ijms22105152
Received: 19 April 2021 / Revised: 7 May 2021 / Accepted: 9 May 2021 / Published: 13 May 2021
(This article belongs to the Special Issue Antibiotic Resistance: Appearance, Evolution, and Spread)
Conjugation, besides transformation and transduction, is one of the main mechanisms of horizontal transmission of genetic information among bacteria. Conjugational transfer, due to its essential role in shaping bacterial genomes and spreading of antibiotics resistance genes, has been widely studied for more than 70 years. However, new and intriguing facts concerning the molecular basis of this process are still being revealed. Most recently, a novel family of conjugative relaxases (Mob proteins) was distinguished. The characteristic feature of these proteins is that they are not related to any of Mobs described so far. Instead of this, they share significant similarity to tyrosine recombinases. In this study MobK—a tyrosine recombinase-like Mob protein, encoded by pIGRK cryptic plasmid from the Klebsiella pneumoniae clinical strain, was characterized. This study revealed that MobK is a site-specific nuclease and its relaxase activity is dependent on both a conserved catalytic tyrosine residue (Y179) that is characteristic of tyrosine recombinases and the presence of Mg2+ divalent cations. The pIGRK minimal origin of transfer sequence (oriT) was also characterized. This is one of the first reports presenting tyrosine recombinase-like conjugative relaxase protein. It also demonstrates that MobK is a convenient model for studying this new protein family. View Full-Text
Keywords: horizontal gene transfer; conjugation; mobile genetic elements; Mob; relaxase; tyrosine recombinase; MobK; pIGRK; Klebsiella pneumoniae; G-quadruplex horizontal gene transfer; conjugation; mobile genetic elements; Mob; relaxase; tyrosine recombinase; MobK; pIGRK; Klebsiella pneumoniae; G-quadruplex
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MDPI and ACS Style

Nowak, K.P.; Sobolewska-Ruta, A.; Jagiełło, A.; Bierczyńska-Krzysik, A.; Kierył, P.; Wawrzyniak, P. Molecular and Functional Characterization of MobK Protein—A Novel-Type Relaxase Involved in Mobilization for Conjugational Transfer of Klebsiella pneumoniae Plasmid pIGRK. Int. J. Mol. Sci. 2021, 22, 5152. https://doi.org/10.3390/ijms22105152

AMA Style

Nowak KP, Sobolewska-Ruta A, Jagiełło A, Bierczyńska-Krzysik A, Kierył P, Wawrzyniak P. Molecular and Functional Characterization of MobK Protein—A Novel-Type Relaxase Involved in Mobilization for Conjugational Transfer of Klebsiella pneumoniae Plasmid pIGRK. International Journal of Molecular Sciences. 2021; 22(10):5152. https://doi.org/10.3390/ijms22105152

Chicago/Turabian Style

Nowak, Katarzyna P.; Sobolewska-Ruta, Agnieszka; Jagiełło, Agata; Bierczyńska-Krzysik, Anna; Kierył, Piotr; Wawrzyniak, Paweł. 2021. "Molecular and Functional Characterization of MobK Protein—A Novel-Type Relaxase Involved in Mobilization for Conjugational Transfer of Klebsiella pneumoniae Plasmid pIGRK" Int. J. Mol. Sci. 22, no. 10: 5152. https://doi.org/10.3390/ijms22105152

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