Overexpression, Biophysical Characterization, and Crystallization of Ribonuclease I from Escherichia coli, a Broad-Specificity Enzyme in the RNase T2 Family

2001 ◽  
Vol 390 (1) ◽  
pp. 42-50 ◽  
Author(s):  
Savita Padmanabhan ◽  
Kangjing Zhou ◽  
Cindy Y. Chu ◽  
Robert W. Lim ◽  
Louis W. Lim
Keyword(s):  
Escherichia Coli ◽  
Biophysical Characterization ◽  
Rnase T2 ◽  
Ribonuclease I ◽  
Broad Specificity

scholarly journals A Broad-Specificity Multidrug Efflux Pump Requiring a Pair of Homologous SMR-Type Proteins

2000 ◽  
Vol 182 (8) ◽  
pp. 2311-2313 ◽  
Author(s):  
Donald L. Jack ◽  
Michael L. Storms ◽  
Jason H. Tchieu ◽  
Ian T. Paulsen ◽  
Milton H. Saier
Keyword(s):  
Escherichia Coli ◽  
Efflux Pump ◽  
Multidrug Resistant ◽  
Drug Efflux ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
Resistant Phenotype ◽  
Small Multidrug Resistance ◽  
Drug Efflux Pumps ◽  
Broad Specificity

ABSTRACT The Bacillus subtilis genome encodes seven homologues of the small multidrug resistance (SMR) family of drug efflux pumps. Six of these homologues are paired in three distinct operons, and coexpression in Escherichia coli of one such operon,ykkCD, but not expression of either ykkC orykkD alone, gives rise to a broad specificity, multidrug-resistant phenotype including resistance to cationic, anionic, and neutral drugs.

scholarly journals Escherichia coli Peptidase A, B, or N Can Process Translation Inhibitor Microcin C

2008 ◽  
Vol 190 (7) ◽  
pp. 2607-2610 ◽  
Author(s):  
Teymur Kazakov ◽  
Gaston H. Vondenhoff ◽  
Kirill A. Datsenko ◽  
Maria Novikova ◽  
Anastasia Metlitskaya ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Growth ◽  
Trna Synthetase ◽  
Methionine Residue ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Translation Inhibitor ◽  
Rate Limiting ◽  
Broad Specificity

ABSTRACT The heptapeptide-nucleotide microcin C (McC) targets aspartyl-tRNA synthetase. Upon its entry into a susceptible cell, McC is processed to release a nonhydrolyzable aspartyl-adenylate that inhibits aspartyl-tRNA synthetase, leading to the cessation of translation and cell growth. Here, we surveyed Escherichia coli cells with singly, doubly, and triply disrupted broad-specificity peptidase genes to show that any of three nonspecific oligopeptidases (PepA, PepB, or PepN) can effectively process McC. We also show that the rate-limiting step of McC processing in vitro is deformylation of the first methionine residue of McC.

scholarly journals An efficient protocol for the production of tRNA-free recombinant Selenocysteine Synthase (SELA) from Escherichia coli and its biophysical characterization

2013 ◽  
Vol 88 (1) ◽  
pp. 80-84 ◽  
Author(s):  
Livia Regina Manzine ◽  
Alexandre Cassago ◽  
Marco Túlio Alves da Silva ◽  
Otavio Henrique Thiemann
Keyword(s):  
Escherichia Coli ◽  
Biophysical Characterization

scholarly journals Biophysical Characterization and Activity of Lymphostatin, a Multifunctional Virulence Factor of Attaching and Effacing Escherichia coli

2016 ◽  
Vol 291 (11) ◽  
pp. 5803-5816 ◽  
Author(s):  
Robin L. Cassady-Cain ◽  
Elizabeth A. Blackburn ◽  
Husam Alsarraf ◽  
Emil Dedic ◽  
Andrew G. Bease ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Virulence Factor ◽  
Biophysical Characterization
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