[HTML][HTML] SRP-mediated protein targeting: structure and function revisited
The signal recognition particle (SRP) and its membrane-bound receptor (SR) deliver
membrane proteins and secretory proteins to the translocation channel in the plasma …
membrane proteins and secretory proteins to the translocation channel in the plasma …
Structural insights into the signal recognition particle
▪ Abstract The signal recognition particle (SRP) directs integral membrane and secretory
proteins to the cellular protein translocation machinery during translation. The SRP is an …
proteins to the cellular protein translocation machinery during translation. The SRP is an …
Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated …
Biologically active proteins without stable ordered structure (ie, intrinsically disordered
proteins) are attracting increased attention. Functional repertoires of ordered and disordered …
proteins) are attracting increased attention. Functional repertoires of ordered and disordered …
Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle
C Oubridge, A Kuglstatter, L Jovine, K Nagai - Molecular cell, 2002 - cell.com
The signal recognition particle (SRP) is a ribonucleoprotein particle involved in GTP-
dependent translocation of secretory proteins across membranes. In Archaea and Eukarya …
dependent translocation of secretory proteins across membranes. In Archaea and Eukarya …
The archaeal Sec–dependent protein translocation pathway
A Bolhuis - … Transactions of the Royal Society of London …, 2004 - royalsocietypublishing.org
Over the past three decades, transport of proteins across cellular membranes has been
studied extensively in various model systems. One of the major transport routes, the so …
studied extensively in various model systems. One of the major transport routes, the so …
Archaea signal recognition particle shows the way
C Zwieb, S Bhuiyan - Archaea, 2010 - Wiley Online Library
Archaea SRP is composed of an SRP RNA molecule and two bound proteins named SRP19
and SRP54. Regulated by the binding and hydrolysis of guanosine triphosphates, the RNA …
and SRP54. Regulated by the binding and hydrolysis of guanosine triphosphates, the RNA …
Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii
I Tozik, Q Huang, C Zwieb, J Eichler - Nucleic acids research, 2002 - academic.oup.com
The signal recognition particle (SRP) is a ribonucleoprotein complex involved in the
recognition and targeting of nascent extracytoplasmic proteins in all three domains of life. In …
recognition and targeting of nascent extracytoplasmic proteins in all three domains of life. In …
Structures of SRP54 and SRP19, the Two Proteins that Organize the Ribonucleic Core of the Signal Recognition Particle from Pyrococcus furiosus
In all organisms the Signal Recognition Particle (SRP), binds to signal sequences of
proteins destined for secretion or membrane insertion as they emerge from translating …
proteins destined for secretion or membrane insertion as they emerge from translating …
[HTML][HTML] Crossing the membrane in Archaea, the third domain of life
D Calo, J Eichler - Biochimica et Biophysica Acta (BBA)-Biomembranes, 2011 - Elsevier
Many of the recent advancements in the field of protein translocation, particularly from the
structural perspective, have relied on Archaea. For instance, the solved structures of the …
structural perspective, have relied on Archaea. For instance, the solved structures of the …
S-domain assembly of the signal recognition particle
AE Sauer-Eriksson, T Hainzl - Current opinion in structural biology, 2003 - Elsevier
The signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein that
associates with ribosomes to mediate the targeting of membrane and secretory proteins to …
associates with ribosomes to mediate the targeting of membrane and secretory proteins to …