@article{oai:iwate-u.repo.nii.ac.jp:00009196,
 author = {Nishiyama, Ken-ichi and Maeda, Masahide and Abe, Masato and Kanamori, Takashi and Shimamoto, Keiko and Kusumoto, Shoichi and Ueda, Takuya and Tokuda, Hajime},
 issue = {3},
 journal = {Biochemical and Biophysical Research Communications},
 month = {Apr},
 note = {A complete reconstitution system for membrane integration of the simplest protein was developed by means of defined factors. A mutant version of Pf3 coat protein, 3L-Pf3 coat, requires neither signal recognition particle/Sec factors nor a membrane potential for its integration into the cytoplasmic membrane of Escherichia coli. Although 3L-Pf3 coat is spontaneously integrated into liposomes composed of phospholipids, diacylglycerol completely blocks such spontaneous integrations at a physiological level. Under the conditions where spontaneous integration does not occur, 3L-Pf3 coat integration was absolutely dependent on a novel integration-stimulating factor. Combination of the PURE system, an in vitro translation system composed of the purified factors involved in translation in E. coli, with liposomes containing the highly purified integration-stimulating factor revealed multiple cycles of 3L-Pf3 coat integration, achieving the complete reconstitution of membrane integration. Based on the function of the factor, we propose that the factor is named MPIase (Membrane Protein Integrase).},
 pages = {733--736},
 title = {A novel complete reconstitution system for membrane integration of the simplest membrane protein},
 volume = {394},
 year = {2010}
}