English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Protein Dynamics in Complex DNA Lesions.

MPS-Authors
/cone/persons/resource/persons219545

Poser,  Ina
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons219341

Krastev,  Dragomir
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons184590

Hubatsch,  Lars
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons219227

Hasse,  Susanne
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons219618

Sarov,  Mihail
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons219042

Buchholz,  Frank
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons219253

Hyman,  Anthony
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons145692

Grill,  Stephan W.
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Aleksandrov, R., Dotchev, A., Poser, I., Krastev, D., Georgiev, G., Panova, G. C., et al. (2018). Protein Dynamics in Complex DNA Lesions. Molecular cell, 69(6), 1046-1061. doi:10.1016/j.molcel.2018.02.016.


Cite as: https://hdl.handle.net/21.11116/0000-0003-F5A1-2
Abstract
A single mutagen can generate multiple different types of DNA lesions. How different repair pathways cooperate in complex DNA lesions, however, remains largely unclear. Here we measured, clustered, and modeled the kinetics of recruitment and dissociation of 70 DNA repair proteins to laser-induced DNA damage sites in HeLa cells. The precise timescale of protein recruitment reveals that error-prone translesion polymerases are considerably delayed compared to error-free polymerases. We show that this is ensured by the delayed recruitment of RAD18 to double-strand break sites. The time benefit of error-free polymerases disappears when PARP inhibition significantly delays PCNA recruitment. Moreover, removal of PCNA from complex DNA damage sites correlates with RPA loading during 5'-DNA end resection. Our systematic study of the dynamics of DNA repair proteins in complex DNA lesions reveals the multifaceted coordination between the repair pathways and provides a kinetics-based resource to study genomic instability and anticancer drug impact.