SRP meets the ribosome.
Cotranslational targeting directly couples synthesis of proteins to their translocation across or insertion into membranes. The signal recognition particle (SRP) and its membrane-bound receptor facilitate the targeting of the translation machinery, the ribosome, via recognition of a signal sequence in the nascent peptide chain. By combining structures of free and ribosome-bound SRP we derive a structural model describing the dynamic nature of SRP when it meets the ribosome.
Wild
Klemens
K
Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
Halic
Mario
M
Sinning
Irmgard
I
Beckmann
Roland
R
D000818:Animals; D018360:Crystallography, X-Ray; D006160:Guanosine Triphosphate / Q000737:chemistry; D006801:Humans; D008954:Models, Biological; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D012270:Ribosomes / Q000378:metabolism / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology; D018271:Signal Recognition Particle / Q000502:physiology; D015398:Signal Transduction; D016944:Sulfolobus / Q000502:physiology
C069268:SRP54 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D018271:Signal Recognition Particle; D006160:Guanosine Triphosphate