scholarly journals Location of protein S1 of Escherichia coli ribosomes at the 'A'-site of the codon binding site. Affinity labeling studies with a 3' -modified A-U-G analog

1976 ◽  
Vol 3 (7) ◽  
pp. 1635-1646 ◽  
Author(s):  
O. Pongs ◽  
G. Stoffler ◽  
R. W. Bald
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Affinity Labeling ◽  
A Site

Affinity labeling of Escherichia coli phenylalanyl-tRNA synthetase at the binding site for tRNAPhe

Biochemistry ◽  
1987 ◽  
Vol 26 (17) ◽  
pp. 5433-5439 ◽  
Author(s):  
Codjo Hountondji ◽  
Jean Marie Schmitter ◽  
Christian Beauvallet ◽  
Sylvain Blanquet
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Trna Synthetase ◽  
Affinity Labeling

Affinity labeling at the A-site of Escherichia coli ribosomes by a non-hydrolyzable γ-amide analog of GTP

Biochimie ◽  
1988 ◽  
Vol 70 (5) ◽  
pp. 597-603 ◽  
Author(s):  
Galina T. Babkina ◽  
Jiří Jonák ◽  
Galina G. Karpova ◽  
Dmitri G. Knorre ◽  
Ivan Rychlík ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Affinity Labeling ◽  
A Site

scholarly journals The BldD Protein from Streptomyces coelicolor Is a DNA-Binding Protein

1999 ◽  
Vol 181 (21) ◽  
pp. 6832-6835 ◽  
Author(s):  
Marie A. Elliot ◽  
Brenda K. Leskiw
Keyword(s):  
Escherichia Coli ◽  
Hydroxyl Radical ◽  
Binding Site ◽  
Promoter Region ◽  
Streptomyces Coelicolor ◽  
Dna Binding Protein ◽  
Mobility Shift ◽  
Gel Mobility Shift ◽  
A Site ◽  
Hydroxyl Radical Footprinting

ABSTRACT Gel mobility shift assays with His-tagged BldD isolated fromEscherichia coli have illustrated that BldD is capable of specifically recognizing its own promoter region. DNase I and hydroxyl radical footprinting assays have served to delimit the BldD binding site, revealing that BldD recognizes and binds to a site just upstream from, and overlapping with, the −10 region of the promoter. How BldD binds to its promoter and the effect this binding has on the expression of BldD are discussed.

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