Signal sequence recognition and protein targeting.
Intracellular traffic is often controlled not by highways, but by handshakes and partner introductions within a cellular network. Recently determined structures suggest how signal sequences are recognized and how the GTP affinities of the signal recognition particle and its receptor are coupled to the targeting of ribosomes to translocational membrane pores. The structure of signal peptidase suggests how it releases functional proteins.
Stroud
R M
RM
S-960 Department of Biochemistry and Biophysics, School of Medicine, University of California, San Francisco CA 94143-0448, USA. stroud@msg.ucsf.edu
Walter
P
P
D001483:Base Sequence; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D011485:Protein Binding; D021382:Protein Sorting Signals / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D012313:RNA / Q000378:metabolism; D018271:Signal Recognition Particle / Q000235:genetics
D021382:Protein Sorting Signals; D011506:Proteins; D018271:Signal Recognition Particle; D012313:RNA; D006160:Guanosine Triphosphate