Results 211 to 220 of about 82,494 (244)

Structural basis of signal-sequence recognition by the signal recognition particle

Nature Structural & Molecular Biology, 2011
The signal recognition particle (SRP) recognizes and binds the signal sequence of nascent proteins as they emerge from the ribosome. We present here the 3.0-Å structure of a signal sequence bound to the Methanococcus jannaschii SRP core. Structural comparison with the free SRP core shows that signal-sequence binding induces formation of the GM-linker ...
Tobias, Hainzl, Shenghua, Huang, Gitte, Meriläinen, Kristoffer, Brännström, A Elisabeth, Sauer-Eriksson   +4 more
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The signal recognition particle in S. cerevisiae

Trends in Cell Biology, 1991
We have identified the Saccharomyces cerevisiae homolog of the signal recognition particle (SRP) and characterized its function in vivo. S. cerevisiae SRP is a 16S particle that includes a homolog of the signal sequence-binding protein subunit of SRP (SRP54p) and a small cytoplasmic RNA (scR1).
B C, Hann, P, Walter
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Structural Insights Into the Signal Recognition Particle

Annual Review of Biochemistry, 2004
▪ Abstract  The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis.
Jennifer A, Doudna, Robert T, Batey
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Functional dissection of the signal recognition particle

Trends in Biochemical Sciences, 1988
Abstract Biochemical mutagenesis — alteration or removal of specific domains within a biological structure — followed by functional analysis, gives insight into structure-function relationships. We describe the analysis of the signal recognition particle, a ribonucleoprotein known to be required for the entry of most proteins into the secretory ...
V, Siegel, P, Walter
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Disassembly and reconstitution of signal recognition particle

Cell, 1983
Signal recognition particle (SRP) is a ribonucleoprotein consisting of six distinct polypeptides and one molecule of small cytoplasmic 7SL-RNA. The particle was previously shown to function in protein translocation across, and protein integration into, the endoplasmic reticulum membrane.
P, Walter, G, Blobel
openaire   +2 more sources

A signal sequence is required for the functions of the signal recognition particle

Biochemical and Biophysical Research Communications, 1986
It is shown that removal of the signal sequence of carp preproinsulin by gene technology abolishes the interaction between the polypeptide chain and the signal recognition particle with respect to both its functions: the inhibition of translation by the signal recognition particle in the absence of microsomal membranes, and the reconstitution of the ...
M, Wiedmann, A, Huth, T A, Rapoport
openaire   +2 more sources

New Insights into Signal Recognition and Elongation Arrest Activities of the Signal Recognition Particle

Biological Chemistry, 1999
AbstractThe signal recognition particle (SRP), a ubiquitous cytoplasmic ribonucleoprotein particle, plays an essential role in promoting co-translational translocation of proteins into the endoplasmic reticulum. Here, we summarise recent progress made in the understanding of two essential SRP functions: the signal recognition function, which ensures ...
Bui, Nazarena, Strub, Katharina
openaire   +2 more sources

The strange case of the signal recognition particle

Nature Reviews Molecular Cell Biology, 2002
The discovery of the signal-recognition particle (SRP) and its receptor represented a huge step forwards in the study of protein translocation and secretion. Just as intriguing was the race to identify SRP, as two teams — one based in New York, the other in Heidelberg — took up the quest and scored complementary victories.
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Signal recognition particle (SRP)

1994
Abstract The particle is comprised of one molecule of 7SL RNA (about 300 nucleotides) and six distinct polypeptides3 The six SRP polypeptide chains are organized into four SRP proteins. These are two monomers, a 19 kDa polypeptide and a 54 kDa polypeptide, and two heterodimers, one composed of a 9 kDa and a 14 kDa polypeptide (p9/14 ...
D L Zimmerman, P Walter
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Signal Recognition Particle

2006
  +4 more sources