scholarly journals The role of changing loop conformations in streptavidin versions engineered for high-affinity binding of the Strep-tag II peptide

2021 ◽  
pp. 166893
Author(s):  
Thomas G.M. Schmidt ◽  
Andreas Eichinger ◽  
Markus Schneider ◽  
Lidia Bonet ◽  
Uwe Carl ◽  
...  
2003 ◽  
Vol 138 (2) ◽  
pp. 325-332 ◽  
Author(s):  
Stephen G Howitt ◽  
Kalle Kilk ◽  
Yang Wang ◽  
David M Smith ◽  
Ulo Langel ◽  
...  

Biochemistry ◽  
1996 ◽  
Vol 35 (43) ◽  
pp. 13833-13842 ◽  
Author(s):  
George M. Willems ◽  
Marie P. Janssen ◽  
Maurice M. A. L. Pelsers ◽  
Paul Comfurius ◽  
Monica Galli ◽  
...  

Peptides ◽  
2001 ◽  
Vol 22 (12) ◽  
pp. 2145-2149 ◽  
Author(s):  
Dieter Knowle ◽  
Jayson Kurfis ◽  
Narasaiah Gavini ◽  
Lakshmidevi Pulakat

1998 ◽  
Vol 53 (1) ◽  
pp. 128-134 ◽  
Author(s):  
Hideo Kikkawa ◽  
Masafumi Isogaya ◽  
Taku Nagao ◽  
Hitoshi Kurose

2000 ◽  
Vol 182 (14) ◽  
pp. 4022-4027 ◽  
Author(s):  
Richard A. Fekete ◽  
Laura S. Frost

ABSTRACT Cleavage at the F plasmid nic site within the origin of transfer (oriT) requires the F-encoded proteins TraY and TraI and the host-encoded protein integration host factor in vitro. We confirm that F TraY, but not F TraM, is required for cleavage atnic in vivo. Chimeric plasmids were constructed which contained either the entire F or R100-1 oriT regions or various combinations of nic, TraY, and TraM binding sites, in addition to the traM gene. The efficiency of cleavage atnic and the frequency of mobilization were assayed in the presence of F or R100-1 plasmids. The ability of these chimeric plasmids to complement an F traM mutant or affect F transfer via negative dominance was also measured using transfer efficiency assays. In cases where cleavage at nic was detected, R100-1 TraI was not sensitive to the two-base difference in sequence immediately downstream of nic, while F TraI was specific for the F sequence. Plasmid transfer was detected only when TraM was able to bind to its cognate sites within oriT. High-affinity binding of TraY in cis to oriTallowed detection of cleavage at nic but was not required for efficient mobilization. Taken together, our results suggest that stable relaxosomes, consisting of TraI, -M, and -Y bound to oriT are preferentially targeted to the transfer apparatus (transferosome).


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