cooperative ordering
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2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Paulo Caldas ◽  
Mar López-Pelegrín ◽  
Daniel J. G. Pearce ◽  
Nazmi Burak Budanur ◽  
Jan Brugués ◽  
...  

AbstractDuring bacterial cell division, the tubulin-homolog FtsZ forms a ring-like structure at the center of the cell. This Z-ring not only organizes the division machinery, but treadmilling of FtsZ filaments was also found to play a key role in distributing proteins at the division site. What regulates the architecture, dynamics and stability of the Z-ring is currently unknown, but FtsZ-associated proteins are known to play an important role. Here, using an in vitro reconstitution approach, we studied how the well-conserved protein ZapA affects FtsZ treadmilling and filament organization into large-scale patterns. Using high-resolution fluorescence microscopy and quantitative image analysis, we found that ZapA cooperatively increases the spatial order of the filament network, but binds only transiently to FtsZ filaments and has no effect on filament length and treadmilling velocity. Together, our data provides a model for how FtsZ-associated proteins can increase the precision and stability of the bacterial cell division machinery in a switch-like manner.


Langmuir ◽  
2016 ◽  
Vol 32 (30) ◽  
pp. 7564-7571 ◽  
Author(s):  
Kevin J. De France ◽  
Kevin G. Yager ◽  
Todd Hoare ◽  
Emily D. Cranston

2015 ◽  
Vol 92 (6) ◽  
Author(s):  
Robert J. Bettles ◽  
Simon A. Gardiner ◽  
Charles S. Adams
Keyword(s):  

2010 ◽  
Vol 114 (5) ◽  
pp. 1810-1814 ◽  
Author(s):  
Douglas M. Scott ◽  
Nickolaus A. Smith ◽  
Joseph J. Valente ◽  
Rachel Adams ◽  
Kevin Bufkin ◽  
...  

Langmuir ◽  
2007 ◽  
Vol 23 (11) ◽  
pp. 6411-6417 ◽  
Author(s):  
F. Gobeaux ◽  
E. Belamie ◽  
G. Mosser ◽  
P. Davidson ◽  
P. Panine ◽  
...  

2004 ◽  
Vol 93 (7) ◽  
Author(s):  
T. Masuda ◽  
A. Zheludev ◽  
B. Grenier ◽  
S. Imai ◽  
K. Uchinokura ◽  
...  

2002 ◽  
Vol 35 (2) ◽  
pp. 233-242 ◽  
Author(s):  
P. M. Woodward ◽  
K. Z. Baba-Kishi

The crystal structure of the relaxor ferroelectric Pb2ScTaO6has been refined from high-resolution neutron time-of-flight powder diffraction data recorded at various temperatures from 4 to 400 K. Upon warming, Pb2ScTaO6undergoes a first-order transition at 295 K from the rhombohedral ferroelectric state into the cubic paraelectric state. At 4.2 K, in the ferroelectric state, this compound adoptsR3 space-group symmetry, witha= 8.15231 (7) Å and α = 89.8488 (3)°. At 400 K, in the paraelectric state, this compound adoptsFm\bar{3}mspace-group symmetry, witha= 8.15345 (3) Å. In the ferroelectric state, the Pb2+coordination polyhedra are quite asymmetric, clearly indicating the presence of a stereoactive electron lone pair. The Sc3+and Ta5+ions are also shifted away from the centers of their respective octahedra, each toward an octahedral face. The large displacement parameters associated with both the Pb and the O ions, in the 400 K structure reveal significant local shifts of these ions from their ideal sites in the paraelectric state. Thus, the paraelectric to ferroelectric transition is driven by long-range cooperative ordering of the cation displacements. Synchrotron X-ray powder diffraction measurements are used to estimate the domain size of the Sc3+/Ta5+ordering and the ferroelectric cation displacements as 88 nm and 10 nm, respectively.


Biochemistry ◽  
2000 ◽  
Vol 39 (33) ◽  
pp. 10045-10054 ◽  
Author(s):  
Janet S. Anderson ◽  
Michael D. Forman ◽  
Sarah Modleski ◽  
Frederick W. Dahlquist ◽  
Susan M. Baxter

1999 ◽  
pp. 2245-2246 ◽  
Author(s):  
Michael A. Leech ◽  
Judith A. K. Howard ◽  
Slimane Dahaoui ◽  
Nayan K. Solanki ◽  
Malcolm A. Halcrow

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