Crystal Structure of the Ribonucleoprotein Core of the Signal Recognition Particle
- 18 February 2000
- journal article
- editorial
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 287 (5456), 1232-1239
- https://doi.org/10.1126/science.287.5456.1232
Abstract
The signal recognition particle (SRP), a protein-RNA complex conserved in all three kingdoms of life, recognizes and transports specific proteins to cellular membranes for insertion or secretion. We describe here the 1.8 angstrom crystal structure of the universal core of the SRP, revealing protein recognition of a distorted RNA minor groove. Nucleotide analog interference mapping demonstrates the biological importance of observed interactions, and genetic results show that this core is functional in vivo. The structure explains why the conserved residues in the protein and RNA are required for SRP assembly and defines a signal sequence recognition surface composed of both protein and RNA.Keywords
This publication has 40 references indexed in Scilit:
- Themes in RNA-protein recognitionJournal of Molecular Biology, 1999
- Crystal Structure of the Conserved Subdomain of Human Protein SRP54M at 2.1Å Resolution: Evidence for the Mechanism of Signal Peptide BindingJournal of Molecular Biology, 1999
- Nucleotide Analog Interference MappingMethods, 1999
- Ribozyme chemogeneticsBiopolymers, 1998
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- Structural Classification of HTH DNA-binding Domains and Protein – DNA Interaction ModesJournal of Molecular Biology, 1996
- Identification of a Region of Bacillus subtilis Ffh, a Homologue of Mammalian SRP54 Protein, That Is Essential for Binding to Small Cytoplasmic RNAPublished by Elsevier ,1996
- The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane.The Journal of cell biology, 1995
- GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocationNature, 1993
- The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain.The Journal of cell biology, 1990