Results 51 to 60 of about 4,057 (206)

YidC from Escherichia coli Forms an Ion-Conducting Pore upon Activation by Ribosomes

open access: yesBiomolecules, 2023
The universally conserved protein YidC aids in the insertion and folding of transmembrane polypeptides. Supposedly, a charged arginine faces its hydrophobic lipid core, facilitating polypeptide sliding along YidC’s surface.
Denis G. Knyazev   +9 more
doaj   +1 more source

Structural basis of Sec-independent membrane protein insertion by YidC [PDF]

open access: yes, 2014
[プレスリリース]バイオサイエンス研究科膜分子複合機能学研究室の塚崎智也准教授らの研究グループが、タンパク質を細胞膜に組み込むメカニズムを解明しました(2014/04/17)Newly synthesized membrane proteins must be accurately inserted into the membrane, folded and assembled for proper functioning. The protein YidC inserts its substrates
Arisaka, Fumio   +18 more
core   +1 more source

Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease [PDF]

open access: yes, 2017
Mitochondria fulfill a diverse range of functions in cells including oxygen metabolism, homeostasis of inorganic ions and execution of apoptosis. Biogenesis of mitochondria relies on protein import pathways that are ensured by dedicated multiprotein ...
MacPherson, Lisa   +1 more
core   +1 more source

Membrane Insertases Are Present in All Three Domains of Life [PDF]

open access: yesStructure, 2015
In this issue of Structure, Borowska et al. (2015) report the crystal structure and provide experimental evidence on an archaeal membrane insertase, the DUF106 protein from Methanocaldococcus jannaschii, demonstrating that YidC/Oxa1/Alb3-like insertases exist in the archaeal plasma membrane.
Dalbey, Ross E., Kuhn, Andreas
openaire   +2 more sources

Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs

open access: yesCommunications Biology, 2020
With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs.
Matthew G. Iadanza   +11 more
doaj   +1 more source

Synthesis of Chlorophyll-Binding Proteins in a Fully Segregated Δycf54 Strain of the Cyanobacterium Synechocystis PCC 6803 [PDF]

open access: yes, 2016
In the chlorophyll (Chl) biosynthesis pathway the formation of protochlorophyllide is catalyzed by Mg-protoporphyrin IX methyl ester (MgPME) cyclase. The Ycf54 protein was recently shown to form a complex with another component of the oxidative cyclase ...
Albus   +51 more
core   +2 more sources

Concerted Complex Assembly and GTPase Activation in the Chloroplast Signal Recognition Particle [PDF]

open access: yes, 2011
The universally conserved signal recognition particle (SRP) and SRP receptor (SR) mediate the cotranslational targeting of proteins to cellular membranes.
Chandrasekar, Sowmya   +4 more
core   +3 more sources

YidC Insertase of Escherichia coli: Water Accessibility and Membrane Shaping [PDF]

open access: yesStructure, 2017
The YidC/Oxa1/Alb3 family of membrane proteins function to insert proteins into membranes in bacteria, mitochondria, and chloroplasts. Recent X-ray structures of YidC from Bacillus halodurans and Escherichia coli revealed a hydrophilic groove that is accessible from the lipid bilayer and the cytoplasm.
Chen, Yuanyuan   +6 more
openaire   +4 more sources

OXA1L mutations cause mitochondrial encephalopathy and a combined oxidative phosphorylation defect

open access: yesEMBO Molecular Medicine, 2018
OXA1, the mitochondrial member of the YidC/Alb3/Oxa1 membrane protein insertase family, is required for the assembly of oxidative phosphorylation complexes IV and V in yeast.
Kyle Thompson   +24 more
doaj   +1 more source

Conformational Flexibility of the Protein Insertase BamA in the Native Asymmetric Bilayer Elucidated by ESR Spectroscopy

open access: yesAngewandte Chemie, 2021
The β‐barrel assembly machinery (BAM) consisting of the central β‐barrel BamA and four other lipoproteins mediates the folding of the majority of the outer membrane proteins. BamA is placed in an asymmetric bilayer and its lateral gate is suggested to be
Aathira Gopinath, B. Joseph
semanticscholar   +1 more source

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