Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments of Deinococcus radiodurans RecA

Autor:	Maksim Serdakov, Aleksandr Alekseev, Galina Cherevatenko, Georgii Pobegalov, Irina V. Bakhlanova, Mikhail Khodorkovskii, Alexander Yakimov, Dmitry M. Baitin
Rok vydání:	2020
Předmět:	0301 basic medicine DNA damage DNA repair RAD51 homologous recombination Eukaryotic DNA replication Catalysis lcsh:Chemistry Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound ATP hydrolysis Physical and Theoretical Chemistry lcsh:QH301-705.5 Deinococcus radiodurans Molecular Biology Spectroscopy RecA 030102 biochemistry & molecular biology biology Organic Chemistry General Medicine biology.organism_classification Computer Science Applications 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 chemistry Biophysics Homologous recombination DNA
Zdroj:	International Journal of Molecular Sciences Volume 21 Issue 19 International Journal of Molecular Sciences, Vol 21, Iss 7389, p 7389 (2020)
ISSN:	1422-0067
DOI:	10.3390/ijms21197389
Popis:	Deinococcus radiodurans (Dr) has one of the most robust DNA repair systems, which is capable of withstanding extreme doses of ionizing radiation and other sources of DNA damage. DrRecA, a central enzyme of recombinational DNA repair, is essential for extreme radioresistance. In the presence of ATP, DrRecA forms nucleoprotein filaments on DNA, similar to other bacterial RecA and eukaryotic DNA strand exchange proteins. However, DrRecA catalyzes DNA strand exchange in a unique reverse pathway. Here, we study the dynamics of DrRecA filaments formed on individual molecules of duplex and single-stranded DNA, and we follow conformational transitions triggered by ATP hydrolysis. Our results reveal that ATP hydrolysis promotes rapid DrRecA dissociation from duplex DNA, whereas on single-stranded DNA, DrRecA filaments interconvert between stretched and compressed conformations, which is a behavior shared by E. coli RecA and human Rad51. This indicates a high conservation of conformational switching in nucleoprotein filaments and suggests that additional factors might contribute to an inverse pathway of DrRecA strand exchange.
Databáze:	OpenAIRE
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