Lentivirus envelope sequences and pro viral genomes are stabilized in Escherichia coli when cloned in low-copy-number plasmid vectors

Gene ◽  
1993 ◽  
Vol 124 (1) ◽  
pp. 93-98 ◽  
Author(s):  
Thomas P. Cunningham ◽  
Ronald C. Montelaro ◽  
Keith E. Rushlow
Gene ◽  
1982 ◽  
Vol 18 (3) ◽  
pp. 335-341 ◽  
Author(s):  
Neil G. Stoker ◽  
Neu F. Fairweathe ◽  
Brian G. Spratt

1982 ◽  
Vol 150 (3) ◽  
pp. 1234-1243 ◽  
Author(s):  
W Firshein ◽  
P Strumph ◽  
P Benjamin ◽  
K Burnstein ◽  
J Kornacki

1986 ◽  
Vol 37 (2) ◽  
pp. 193-197 ◽  
Author(s):  
Hilde Reuse ◽  
Eliette Touati ◽  
Philippe Glaser ◽  
Antoine Danchin

Gene ◽  
1987 ◽  
Vol 61 (1) ◽  
pp. 63-74 ◽  
Author(s):  
Sunao Takeshita ◽  
Masahiro Sato ◽  
Mari Toba ◽  
Wakako Masahashi ◽  
Tamotsu Hashimoto-Gotoh

2018 ◽  
Vol 115 (13) ◽  
pp. 3458-3463 ◽  
Author(s):  
Andrzej Szewczak-Harris ◽  
Jan Löwe

Low copy-number plasmid pLS32 ofBacillus subtilissubsp.nattocontains a partitioning system that ensures segregation of plasmid copies during cell division. The partitioning locus comprises actin-like protein AlfA, adaptor protein AlfB, and the centromeric sequenceparN. Similar to the ParMRC partitioning system fromEscherichia coliplasmid R1, AlfA filaments form actin-like double helical filaments that arrange into an antiparallel bipolar spindle, which attaches its growing ends to sister plasmids through interactions with AlfB andparN. Because, compared with ParM and other actin-like proteins, AlfA is highly diverged in sequence, we determined the atomic structure of nonbundling AlfA filaments to 3.4-Å resolution by cryo-EM. The structure reveals how the deletion of subdomain IIB of the canonical actin fold has been accommodated by unique longitudinal and lateral contacts, while still enabling formation of left-handed, double helical, polar and staggered filaments that are architecturally similar to ParM. Through cryo-EM reconstruction of bundling AlfA filaments, we obtained a pseudoatomic model of AlfA doublets: the assembly of two filaments. The filaments are antiparallel, as required by the segregation mechanism, and exactly antiphasic with near eightfold helical symmetry, to enable efficient doublet formation. The structure of AlfA filaments and doublets shows, in atomic detail, how deletion of an entire domain of the actin fold is compensated by changes to all interfaces so that the required properties of polymerization, nucleotide hydrolysis, and antiparallel doublet formation are retained to fulfill the system’s biological raison d’être.


Plasmid ◽  
2008 ◽  
Vol 59 (1) ◽  
pp. 1-10 ◽  
Author(s):  
David Šmajs ◽  
Michal Strouhal ◽  
Petra Matějková ◽  
Darina Čejková ◽  
Luciana Cursino ◽  
...  

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