@phdthesis{oai:tsukuba.repo.nii.ac.jp:00008352,
 author = {掛下, 大視 and Kakeshita, Hiroshi},
 month = {},
 note = {In mammalian cellls, the signal recognition particle(SRP) and the SRP receptor play a central role in targeting presecretory proteins to the membrane of the endoplasmic reticulum(ER). SRP is a ribonucleo-protein complex composed of one RNA(SRP 7S RNA) molecule and six proteins of 9, 14, 19, 54, 68, and 72 kDa. SRP interacts with the signal sequence of nascent polypeptide emerging from ribosomes and the complex formed is targeted and bound to a hetero-dimeric receptor consisting of SRα and SRβ on the ER. In contrast, it has been considered that the chaperones and Sec proteins play a pivotal role in targeting and translocation of secretory proteins in Escherichia coli. However, recently, the molecular homologues to the components of mammalian SRP have been identified in prokaryotes. In E. coli, 4.5S RNA and E. coli Ffh protein have been identified as homologues to the SRP 7S RNA and SRP54 of mammalian SRP, respectively. Furthermore, FtsY exhibits a homology with SRα. In Bacillus subtilis, small cytoplasmic RNA(scRNA) and B. subtilis Ffh protein have been also identified as homologues to the SRP 7S RNA and SRP54, respectively. Depletion of either the SRP RNA or SRP54 homologues ･･･, 2000, Includes bibliographical references},
 school = {筑波大学, University of Tsukuba},
 title = {Molecular and biochemical studies of the Bacillus subtilis FtsY protein, a homologue of the α subunit of mammalian signal recognition particle},
 year = {2001}
}