An improved smaller biotin ligase for BioID proximity labeling
DI Kim, SC Jensen, KA Noble, B Kc… - Molecular biology of …, 2016 - Am Soc Cell Biol
Molecular biology of the cell, 2016•Am Soc Cell Biol
The BioID method uses a promiscuous biotin ligase to detect protein–protein associations
as well as proximate proteins in living cells. Here we report improvements to the BioID
method centered on BioID2, a substantially smaller promiscuous biotin ligase. BioID2
enables more-selective targeting of fusion proteins, requires less biotin supplementation,
and exhibits enhanced labeling of proximate proteins. Thus BioID2 improves the efficiency
of screening for protein–protein associations. We also demonstrate that the biotinylation …
as well as proximate proteins in living cells. Here we report improvements to the BioID
method centered on BioID2, a substantially smaller promiscuous biotin ligase. BioID2
enables more-selective targeting of fusion proteins, requires less biotin supplementation,
and exhibits enhanced labeling of proximate proteins. Thus BioID2 improves the efficiency
of screening for protein–protein associations. We also demonstrate that the biotinylation …
The BioID method uses a promiscuous biotin ligase to detect protein–protein associations as well as proximate proteins in living cells. Here we report improvements to the BioID method centered on BioID2, a substantially smaller promiscuous biotin ligase. BioID2 enables more-selective targeting of fusion proteins, requires less biotin supplementation, and exhibits enhanced labeling of proximate proteins. Thus BioID2 improves the efficiency of screening for protein–protein associations. We also demonstrate that the biotinylation range of BioID2 can be considerably modulated using flexible linkers, thus enabling application-specific adjustment of the biotin-labeling radius.
Am Soc Cell Biol