Results 111 to 120 of about 3,879 (192)

Single rRNA Helices Bind Independently to the Protein‐Conducting Channel SecYEG [PDF]

open access: yesTraffic, 2013
Ribosomes tightly interact with protein‐conducting channels in the plasma membrane of bacteria (SecYEG) and in the endoplasmic reticulum of eukaryotes (Sec61 complex). This interaction is mediated by multiple junctions and is highly conserved during evolution.
Behrens, Christina   +2 more
openaire   +3 more sources

Interaction of secretory protein SecA with its binding partners : lipids and SecB [PDF]

open access: yes
Dissertation supervisor: Dr. Linda Randall.Includes vita.Thirty percent of proteins synthesized in the cytoplasm of E.coli are exported across or into the cytoplasmic membrane to reach their final destinations.
Findik, Bahar Tuba, 1984-
core   +1 more source

Decatransin, a novel natural product inhibiting protein translocation at the Sec61/SecY translocon [PDF]

open access: yes, 2015
A new cyclic decadepsipeptide was isolated from Chaetosphaeria tulasneorum with potent bioactivity on mammalian and yeast cells. Chemogenomic profiling in S.
Junne, Tina   +23 more
core   +4 more sources

Yeast mitochondria can process de novo designed β‐barrel proteins

open access: yesThe FEBS Journal, Volume 291, Issue 2, Page 292-307, January 2024.
Mitochondrial outer membrane β‐barrel proteins are encoded in the nucleus, translated in the cytosol and finally targeted to the organelle. We show that two de novo designed β‐barrel proteins can be expressed in S. cerevisiae, where they are targeted to mitochondria and integrated into the organelle's outer membrane.
Anasuya Moitra   +2 more
wiley   +1 more source

Ion Conductivity of the Bacterial Translocation Channel SecYEG Engaged in Translocation [PDF]

open access: yesJournal of Biological Chemistry, 2014
While engaged in protein transport, the bacterial translocon SecYEG must maintain the membrane barrier to small ions. The preservation of the proton motif force was attributed to (i) cation exclusion, (ii) engulfment of the nascent chain by the hydrophobic pore ring, and (iii) a half-helix partly plugging the channel.
Knyazev, Denis G.   +4 more
openaire   +2 more sources

Membrane Insertion of C-tail Anchored Proteins [PDF]

open access: yes, 2006
The correct localization of proteins is essential for cell viability. In order to achieve correct protein localization to cellular membranes, conserved membrane targeting and translocation mechanisms have evolved.
Yabal, Monica
core  

Anionic phospholipids and the Albino3 translocase activate SRP-receptor interaction during LHCP targeting [PDF]

open access: yes, 2016
The universally conserved signal recognition particle (SRP) co-translationally delivers newly synthesized membrane and secretory proteins to the target cellular membrane.
Chandrasekar, Sowmya, Shan, Shu-ou
core   +2 more sources

Structure of the Oligosaccharyl Transferase Complex at 12 Å Resolution [PDF]

open access: yes, 2003
SummaryOligosaccharyl transferase (OT) catalyzes the transfer of a lipid-linked oligosaccharide to the nascent polypeptide emerging from the translocon. Currently, there is no structural information on the membrane-embedded OT complex, which consists of ...
Li, Hua   +4 more
core   +1 more source

A Broad‐Spectrum Horizontal Transfer Inhibitor Prevents Transmission of Plasmids Carrying Multiple Antibiotic Resistance Genes

open access: yesTransboundary and Emerging Diseases, Volume 2024, Issue 1, 2024.
The dissemination of antimicrobial resistance (AMR) severely degrades the performance of antibiotics and constantly paralyzes the global health system. In particular, plasmid‐mediated transfer of antibiotic resistance genes (ARGs) across bacteria is recognized as the primary driver.
Yuqian Jia   +6 more
wiley   +1 more source

Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in Escherichia coli

open access: yesJournal of Biological Chemistry, 2019
The SecYEG translocon constitutes the major protein transport channel in bacteria and transfers an enormous variety of different secretory and inner-membrane proteins. The minimal core of the SecYEG translocon consists of three inner-membrane proteins, SecY, SecE, and SecG, which, together with appropriate targeting factors, are sufficient for protein ...
Benjamin Jauss   +8 more
openaire   +3 more sources

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