Functional characterization of two anti-estradiol antibodies as deduced from modelling and site-directed mutagenesis experiments

2001 ◽  
Vol 14 (2) ◽  
pp. 99-109 ◽  
Author(s):  
Florence Bettsworth ◽  
C�line Monnet ◽  
B�n�dicte Watelet ◽  
Nicole Battail-Poirot ◽  
Bernard Gilquin ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

scholarly journals Functional Characterization of the N-glycosylation Sites of Human Acid Sphingomyelinase by Site-Directed Mutagenesis

1997 ◽  
Vol 243 (1-2) ◽  
pp. 511-517 ◽  
Author(s):  
Klaus Ferlinz ◽  
Robert Hurwitz ◽  
Heidi Moczall ◽  
Stephanie Lansmann ◽  
Edward H. Schuchman ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Acid Sphingomyelinase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Glycosylation Sites ◽  
Human Acid

scholarly journals Functional Characterization of the mazEF Toxin-Antitoxin System in the Pathogenic Bacterium Agrobacterium tumefaciens

2021 ◽  
Vol 9 (5) ◽  
pp. 1107
Author(s):  
Wonho Choi ◽  
Yoshihiro Yamaguchi ◽  
Ji-Young Park ◽  
Sang-Hyun Park ◽  
Hyeok-Won Lee ◽  
...  
Keyword(s):  
Agrobacterium Tumefaciens ◽  
Physiological Function ◽  
Functional Characterization ◽  
Site Directed Mutagenesis ◽  
In Vitro Assays ◽  
Cell Growth Inhibition ◽  
The Right

Agrobacterium tumefaciens is a pathogen of various plants which transfers its own DNA (T-DNA) to the host plants. It is used for producing genetically modified plants with this ability. To control T-DNA transfer to the right place, toxin-antitoxin (TA) systems of A. tumefaciens were used to control the target site of transfer without any unintentional targeting. Here, we describe a toxin-antitoxin system, Atu0939 (mazE-at) and Atu0940 (mazF-at), in the chromosome of Agrobacterium tumefaciens. The toxin in the TA system has 33.3% identity and 45.5% similarity with MazF in Escherichia coli. The expression of MazF-at caused cell growth inhibition, while cells with MazF-at co-expressed with MazE-at grew normally. In vivo and in vitro assays revealed that MazF-at inhibited protein synthesis by decreasing the cellular mRNA stability. Moreover, the catalytic residue of MazF-at was determined to be the 24th glutamic acid using site-directed mutagenesis. From the results, we concluded that MazF-at is a type II toxin-antitoxin system and a ribosome-independent endoribonuclease. Here, we characterized a TA system in A. tumefaciens whose understanding might help to find its physiological function and to develop further applications.

Sign in / Sign up

Export Citation Format

Share Document