scholarly journals Special Issue: DNA Helicases: Mechanisms, Biological Pathways, and Disease Relevance

Genes ◽  
2021 ◽  
Vol 12 (3) ◽  
pp. 356
Author(s):  
Robert M. Brosh

DNA helicases have emerged as a prominent class of nucleic acid-metabolizing enzymes that play important roles in genome maintenance and cellular homeostasis [...]

2021 ◽  
Vol 11 (8) ◽  
pp. 3594
Author(s):  
Tamaki Endoh ◽  
Eriks Rozners ◽  
Takashi Ohtsuki

Nucleic acids not only store genetic information in their primary sequence but also exhibit biological functions through the formation of their unique structures [...]


2009 ◽  
Vol 186 (5) ◽  
pp. 655-663 ◽  
Author(s):  
Kasper Fugger ◽  
Martin Mistrik ◽  
Jannie Rendtlew Danielsen ◽  
Christoffel Dinant ◽  
Jacob Falck ◽  
...  

Homologous recombination (HR) is essential for faithful repair of DNA lesions yet must be kept in check, as unrestrained HR may compromise genome integrity and lead to premature aging or cancer. To limit unscheduled HR, cells possess DNA helicases capable of preventing excessive recombination. In this study, we show that the human Fbh1 (hFbh1) helicase accumulates at sites of DNA damage or replication stress in a manner dependent fully on its helicase activity and partially on its conserved F box. hFbh1 interacted with single-stranded DNA (ssDNA), the formation of which was required for hFbh1 recruitment to DNA lesions. Conversely, depletion of endogenous Fbh1 or ectopic expression of helicase-deficient hFbh1 attenuated ssDNA production after replication block. Although elevated levels of hFbh1 impaired Rad51 recruitment to ssDNA and suppressed HR, its small interfering RNA–mediated depletion increased the levels of chromatin-associated Rad51 and caused unscheduled sister chromatid exchange. Thus, by possessing both pro- and anti-recombinogenic potential, hFbh1 may cooperate with other DNA helicases in tightly controlling cellular HR activity.


2011 ◽  
Vol 39 (2) ◽  
pp. 413-423 ◽  
Author(s):  
Mark S. Dillingham

Helicases are a ubiquitous and abundant group of motor proteins that couple NTP binding and hydrolysis to processive unwinding of nucleic acids. By targeting this activity to a wide range of specific substrates, and by coupling it with other catalytic functionality, helicases fulfil diverse roles in virtually all aspects of nucleic acid metabolism. The present review takes a look back at our efforts to elucidate the molecular mechanisms of UvrD-like DNA helicases. Using these well-studied enzymes as examples, we also discuss how helicases are programmed by interactions with partner proteins to participate in specific cellular functions.


Nanomaterials ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 951 ◽  
Author(s):  
Justin R. Halman ◽  
Kirill A. Afonin

The use of nucleic acids (RNA and DNA) offers a unique and multifunctional platform for numerous applications including therapeutics, diagnostics, nanodevices, and materials [...]


Sign in / Sign up

Export Citation Format

Share Document