Protein–protein interactions mapped by artificial proteases: where σ factors bind to RNA polymerase

Interactions between proteins are important to understand but difficult to study. Conjugating a protein to a small artificial protease endows it with the ability to cut other proteins where it binds to them. Analysing the sites cut on the target proteins leads to new understanding of the structure o...

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Bibliographic Details
Published in:Trends in biochemical sciences (Amsterdam. Regular ed.) 2000-09, Vol.25 (9), p.408-414
Main Authors: Datwyler, Saul A., Meares, Claude F.
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Blotting, Western
Cysteine - chemistry
Cysteine - metabolism
DNA-Directed RNA Polymerases - chemistry
DNA-Directed RNA Polymerases - metabolism
Edetic Acid - analogs & derivatives
Edetic Acid - chemistry
Edetic Acid - metabolism
Electrophoresis, Polyacrylamide Gel
Endopeptidases - chemistry
Endopeptidases - metabolism
FeBABE
Footprinting
Iron Chelating Agents - chemistry
Iron Chelating Agents - metabolism
Iron-EDTA
Models, Chemical
Models, Molecular
Organometallic Compounds - chemistry
Organometallic Compounds - metabolism
Protein Binding
Protein cleavage
Protein Structure, Secondary
proteinase
RNA polymerase
Sigma
Sigma Factor - chemistry
Sigma Factor - metabolism
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Summary:Interactions between proteins are important to understand but difficult to study. Conjugating a protein to a small artificial protease endows it with the ability to cut other proteins where it binds to them. Analysing the sites cut on the target proteins leads to new understanding of the structure of each complex. The binding of σ factors to a common region on RNA polymerase provides an example.
ISSN:0968-0004
1362-4326
DOI:10.1016/S0968-0004(00)01652-2