Results 61 to 70 of about 3,879 (192)
Cell Reports, 2022 Summary: Protein machines undergo conformational motions to interact with and manipulate polymeric substrates. The Sec translocase promiscuously recognizes, becomes activated, and secretes >500 non-folded preprotein clients across bacterial cytoplasmic ...
Srinath Krishnamurthy +10 more
doaj +1 more source
The integration of YidC into the cytoplasmic membrane of Escherichia coli requires the signal recognition particle, SecA and SecYEG [PDF]
, 2002 The integration of the polytopic membrane protein YidC into the inner membrane of Escherichia coli was analyzed employing an in vitro system. Upon integration of in vitro synthesized YidC, a 42-kDa membrane protected fragment was detected, which could be
Koch, H. G. +3 more
core +2 more sources
A Distinct Mechanism to Achieve Efficient Signal Recognition Particle (SRP)-SRP Receptor Interaction by the Chloroplast SRP Pathway [PDF]
, 2009 Cotranslational protein targeting by the signal recognition particle (SRP) requires the SRP RNA, which accelerates the interaction between the SRP and SRP receptor 200-fold.
Jaru-Ampornpan, Peera +2 more
core +2 more sources
Charge-driven dynamics of nascent-chain movement through the SecYEG translocon [PDF]
Nature Structural & Molecular Biology, 2015 On average, every fifth residue in secretory proteins carries either a positive or a negative charge. In a bacterium such as Escherichia coli, charged residues are exposed to an electric field as they transit through the inner membrane, and this should generate a fluctuating electric force on a translocating nascent chain.
Nurzian Ismail +3 more
openaire +3 more sources
SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase [PDF]
Journal of Biological Chemistry, 1995 The transport of large preproteins across the Escherichia coli plasma membrane is catalyzed by preprotein translocase, comprised of the peripherally bound SecA subunit and an integrally bound heterotrimeric domain consisting of the SecY, SecE, and SecG subunits.
K, Douville +4 more
openaire +2 more sources
Ribosome–SRP–FtsY cotranslational targeting complex in the closed state [PDF]
, 2015 The signal recognition particle (SRP)-dependent pathway is essential for correct targeting of proteins to the membrane and subsequent insertion in the membrane or secretion.
Ariosa, Aileen +7 more
core +1 more source
SecY-SecA fusion protein retains the ability to mediate protein transport. [PDF]
PLoS ONE, 2017 In bacteria, the membrane protein complex SecY/E/G and SecA ATPase are essential for protein translocation. About 30% of newly synthesized proteins in the cytosol are targeted to and translocated across the cytoplasmic membrane by the Sec factors ...
Yasunori Sugano +4 more
doaj +1 more source
Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence. [PDF]
, 2017 The bacterial signal recognition particle (SRP) is part of the machinery that targets ribosomes synthesizing membrane proteins to membrane-embedded translocons co-translationally. Recognition of nascent membrane proteins occurs by virtue of a hydrophobic
Holtkamp, W. +3 more
core +2 more sources
ChemBioChem, Volume 26, Issue 9, May 5, 2025.Regulated intramembrane proteolysis is crucial for functional proteome in all kingdoms of life. The task of cleaving transmembrane proteins within the unique environment of the lipid bilayer presents biochemical challenges that has been solved by integral membrane proteases (IMPRs).
Hannah Fremlén, Björn M. Burmann
wiley +1 more source
Viruses, 2021 The minor coat protein G3p of bacteriophage M13 is the key component for the host interaction of this virus and binds to Escherichia coli at the tip of the F pili.
Farina Kleinbeck, Andreas Kuhn
doaj +1 more source