8-Br-GTP, an analog of GTP, functions as both a competitive inhibitor of FtsZ polymerization and GTPase activity (with a K i value of 31.8 μM). Moreover, it is capable of facilitating nucleic acid modification.
Using specific antisera raised against synthetic peptides, we find that three distinct GTP-binding protein alpha subunits remain bound to the plasma membrane even after activation with nonhydrolyzable GTP analog. Trypsin cleaves each alpha subunit at a si