TY  - JOUR
TI  - Co-immunoprecipitation in Yeast
AU  - Panasenko, Olesya O.
VL  - 2
IS  - 16
PY  - 2012
DA  - 2012/08/20
SP  - e250
C1  - Bio-protocol 2012;2:e250
DO  - 10.21769/BioProtoc.250
UR  - https://doi.org/10.21769/BioProtoc.250
AB  - This protocol describes investigation of protein-protein interactions in baker yeast by co-immunoprecipitation (CoIP). CoIP is a technique to identify physiologically relevant protein-protein interactions in the cell. The interesting protein can be isolated out of solution using antibody that specifically binds to that particular protein (antigene protein). The partner proteins that are bound to a specific target protein can be co-immunoprecipitated together with an antigen. These protein complexes can then be analyzed to identify new binding partners, binding affinities, the kinetics of binding and the function of the target protein. Here I describe the protocols that allow to immunoprecipitate different protein complexes, for example NAC complex (Panasenko et al., 2009), Ccr4-Not complex (Panasenko and Collort, 2011), ribosomes (Panasenko and Collort, 2012) and investigate their partners. For each CoIP I used the different lysis buffer, as indicated below in recipes.
KW  - Immunoprecipitation
KW  - Protein interaction
KW  - Affinity interaction
KW  - Antibody
KW  - Yeast
JF  - Bio-protocol
SN  - 2331-8325
PB  - Bio-protocol LLC.
BIO101  - False