Signal sequence recognition and protein targeting

R M Stroud; P Walter

doi:10.1016/s0959-440x(99)00040-8

Signal sequence recognition and protein targeting

Curr Opin Struct Biol. 1999 Dec;9(6):754-9. doi: 10.1016/s0959-440x(99)00040-8.

Authors

R M Stroud¹, P Walter

Affiliation

¹ S-960 Department of Biochemistry and Biophysics, School of Medicine, University of California, San Francisco CA 94143-0448, USA. stroud@msg.ucsf.edu

PMID: 10607673
DOI: 10.1016/s0959-440x(99)00040-8

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

MeSH terms

Base Sequence
Biological Transport
Cell Membrane / metabolism
Guanosine Triphosphate / metabolism
Protein Binding
Protein Sorting Signals / metabolism*
Proteins / metabolism*
RNA / metabolism
Signal Recognition Particle / genetics

Substances

Protein Sorting Signals
Proteins
Signal Recognition Particle
RNA
Guanosine Triphosphate