Progress Towards the Anatomy of the Eukaryotic DNA Replication Fork

Author(s):  
Heinz Peter Nasheuer ◽  
Helmut Pospiech ◽  
Juhani Syväoja
2010 ◽  
Vol 107 (41) ◽  
pp. 17674-17679 ◽  
Author(s):  
Andres A. Larrea ◽  
Scott A. Lujan ◽  
Stephanie A. Nick McElhinny ◽  
Piotr A. Mieczkowski ◽  
Michael A. Resnick ◽  
...  

Genes ◽  
2018 ◽  
Vol 9 (12) ◽  
pp. 622 ◽  
Author(s):  
Louis-Alexandre Fournier ◽  
Arun Kumar ◽  
Peter Stirling

Eukaryotic DNA replication occurs in the context of chromatin. Recent years have seen major advances in our understanding of histone supply, histone recycling and nascent histone incorporation during replication. Furthermore, much is now known about the roles of histone remodellers and post-translational modifications in replication. It has also become clear that nucleosome dynamics during replication play critical roles in genome maintenance and that chromatin modifiers are important for preventing DNA replication stress. An understanding of how cells deploy specific nucleosome modifiers, chaperones and remodellers directly at sites of replication fork stalling has been building more slowly. Here we will specifically discuss recent advances in understanding how chromatin composition contribute to replication fork stability and restart.


2008 ◽  
Vol 284 (7) ◽  
pp. 4041-4045 ◽  
Author(s):  
Peter M. J. Burgers

2013 ◽  
Vol 454 (2) ◽  
pp. 333-343 ◽  
Author(s):  
Roberta Di Perna ◽  
Valentina Aria ◽  
Mariarosaria De Falco ◽  
Vincenzo Sannino ◽  
Andrei L. Okorokov ◽  
...  

The eukaryotic DNA replication protein Mcm10 (mini-chromosome maintenance 10) associates with chromatin in early S-phase and is required for assembly and function of the replication fork protein machinery. Another essential component of the eukaryotic replication fork is Cdc45 (cell division cycle 45), which is required for both initiation and elongation of DNA replication. In the present study we characterize, for the first time, the physical and functional interactions of human Mcm10 and Cdc45. First we demonstrated that Mcm10 and Cdc45 interact in cell-free extracts. We then analysed the role of each of the Mcm10 domains: N-terminal, internal and C-terminal (NTD, ID and CTD respectively). We have detected a direct physical interaction between CTD and Cdc45 by both in vitro co-immunoprecipitation and surface plasmon resonance experiments. On the other hand, we have found that the interaction of the Mcm10 ID with Cdc45 takes place only in the presence of DNA. Furthermore, we found that the isolated ID and CTD domains are fully functional, retaining DNA-binding capability with a clear preference for bubble and fork structures, and that they both enhance Cdc45 DNA-binding affinity. The results of the present study demonstrate that human Mcm10 and Cdc45 directly interact and establish a mutual co-operation in DNA binding.


1997 ◽  
Vol 272 (8) ◽  
pp. 4647-4650 ◽  
Author(s):  
Robert A. Bambara ◽  
Richard S. Murante ◽  
Leigh A. Henricksen

Physiology ◽  
1997 ◽  
Vol 12 (3) ◽  
pp. 125-131
Author(s):  
U Hubscher ◽  
JM Sogo

Before a cell divides into two identical daughter cells, the entire genome must be replicated faithfully. The mechanistic details of this complex macromolecular process, called DNA replication, have recently been clarified. We focus on the current knowledge at the eukaryotic DNA replication fork at the levels of DNA and chromatin.


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