Signal recognition particle (SRP), a ubiquitous initiator of protein translocation

H Lütcke - European journal of biochemistry, 1995 - Wiley Online Library
In higher eukaryotes, most secretory and membrane proteins are synthesised by ribosomes
which are attached to the membrane of the rough endoplasmic reticulum (RER). This allows …

Antibody to signal recognition particle in polymyositis

IN Targoff, AE Johnson, FW Miller - Arthritis & Rheumatism …, 1990 - Wiley Online Library
Using immunoprecipitation, we identified 13 patients with antibodies to the signal
recognition particle (SRP) from a collection of sera representing 265 poly‐myositis …

Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle

HD Bernstein, MA Poritz, K Strub, PJ Hoben, S Brenner… - Nature, 1989 - nature.com
PROTEIN targeting to the endoplasmic reticulum in mammalian cells is catalysed by signal
recognition particle (SRP) 1, 2. Cross-linking experiments have shown that the subunit of …

Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process

MH Saier Jr, PK Werner, M Müller - Microbiological reviews, 1989 - Am Soc Microbiol
334 SAIER ET AL. ally similar (see sections III and V). Cleavage of amino-terminal signal
sequences by signal peptidases occurs with similar specificities (89, 184, 220, 322); the …

The methionine‐rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence.

D Zopf, HD Bernstein, AE Johnson, P Walter - The EMBO journal, 1990 - embopress.org
The 54 kd protein subunit of the signal recognition particle (SRP54) has been shown to bind
signal sequences by UV crosslinking. Primary structure analysis and phylogenetic …

Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP–binding domains

K Römisch, J Webb, J Herz, S Prehn, R Frank… - Nature, 1989 - nature.com
MOST proteins exported from mammalian cells contain a signal sequence which mediates
targeting to and insertion into the mem-brane of the endoplasmic reticulum (ER) 1, 2 …

Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP

V Siegel, P Walter - Cell, 1988 - cell.com
Signal recognition particle (SRP), a small ribonucleoprotein required for targeting secretory
proteins to the ER, has three known functions: signal recognition, elongation arrest, and …

The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain.

K Römisch, J Webb, K Lingelbach… - The Journal of cell …, 1990 - rupress.org
Signal recognition particle (SRP) plays the key role in targeting secretory proteins to the
membrane of the endoplasmic reticulum (Walter, P., and VR Lingappa. 1986. Annu. Rev …

Binding Sites of the 9- and 14-Kilodalton Heterodimeric Protein Subunit of the Signal Recognition Particle (SRP) Are Contained Exclusively in the Alu Domain of SRP …

K Strub, J Moss, P Walter - Molecular and Cellular Biology, 1991 - Taylor & Francis
The mammalian signal recognition particle (SRP) is a small cytoplasmic ribonucleoprotein
required for the cotranslational targeting of secretory proteins to the endoplasmic reticulum …

Asna1/TRC40-mediated membrane insertion of tail-anchored proteins

V Favaloro, F Vilardi, R Schlecht… - Journal of cell …, 2010 - journals.biologists.com
Tail-anchored (TA) proteins insert post-translationally into the membrane of the endoplasmic
reticulum (ER) and span the membrane by their C-terminal transmembrane domain. We …