Nucleic Acids Research, Vol 27, Issue 4 919-929, Copyright © 1999 by Oxford University Press
M Vidal and P Legrain
Since its original description almost 10 years ago, the yeast two- hybrid
system has been used extensively to identify protein-protein interactions
from many different organisms. Simultaneously, a number of 'variations on a
theme' based on the original concept have been described. In one set of
variations, systems were developed to detect other macromolecular
interactions: DNA-protein (one-hybrid), RNA- protein (RNA-based
three-hybrid) and small molecule-protein interactions (ligand-based
three-hybrid). These different versions are collectively referred to here
as 'n-hybrid systems'. In another set of variations, the original
configuration of the two-hybrid fusion proteins was modified to expand the
range of possible protein-protein interactions that could be analyzed. For
example, systems were developed to detect trimeric interactions,
ligand-receptor interactions or interactions that require particular
post-translational modifications. Finally, the original concept was turned
upside down and 'reverse n-hybrid systems' were developed to identify
mutations, peptides or small molecules that dissociate macromolecular
interactions. These reagents can be used to validate, in the relevant
biological systems, the potential interactions identified with the 'forward
n-hybrid systems'. The powerful genetic selections of the forward and
reverse n-hybrid systems are proving useful in proteomic projects aimed at
generating macromolecular interaction maps.
REVIEWS
Yeast forward and reverse 'n'-hybrid systems
MGH Cancer Center, Charlestown, MA 02129, USA. vidal@helix.mgh.harvard.edu
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