The nucleoid protein Dps binds genomic DNA of Escherichia coli in a non-random manner.
Dps is a multifunctional homododecameric protein that oxidizes Fe2+ ions accumulating them in the form of Fe2O3 within its protein cavity, interacts with DNA tightly condensing bacterial nucleoid upon starvation and performs some other functions. During the last two decades from discovery of this pr...
Main Authors: | S S Antipov, M N Tutukina, E V Preobrazhenskaya, F A Kondrashov, M V Patrushev, S V Toshchakov, I Dominova, U S Shvyreva, V V Vrublevskaya, O S Morenkov, N A Sukharicheva, V V Panyukov, O N Ozoline |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2017-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC5553809?pdf=render |
Similar Items
-
Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy.
by: Vladislav V Melekhov, et al.
Published: (2015-01-01) -
The Oligomeric Form of the Escherichia coli Dps Protein Depends on the Availability of Iron Ions
by: Sergey Antipov, et al.
Published: (2017-11-01) -
High resolution cryogenic transmission electron microscopy study of Escherichia coli Dps protein: First direct observation in quasinative state
by: S.S. Antipov, et al.
Published: (2018-12-01) -
Promoters of Escherichia coli versus promoter islands: function and structure comparison.
by: Valeriy V Panyukov, et al.
Published: (2013-01-01) -
Unveiling the role of Dps in the organization of mycobacterial nucleoid.
by: Payel Ghatak, et al.
Published: (2011-01-01)