Results 61 to 70 of about 4,057 (206)

Signal Recognition Particle: An Essential Protein-Targeting Machine [PDF]

open access: yes, 2013
The signal recognition particle (SRP) and its receptor compose a universally conserved and essential cellular machinery that couples the synthesis of nascent proteins to their proper membrane localization. The past decade has witnessed an explosion in
Akopian, David   +3 more
core   +1 more source

Protein insertion into the inner membrane of mitochondria: routes and mechanisms. [PDF]

open access: yesFEBS Open Bio
Proteins of the inner membrane of mitochondria can embark on three distinct import pathways that direct them into the inner membrane. This review describes the machinery and mechanisms by which proteins are inserted into the inner membrane by the TIM22 complex from the intermembrane space, by lateral insertion from the TIM23 complex or by conservative ...
Kizmaz B, Nutz A, Egeler A, Herrmann JM.
europepmc   +2 more sources

COA6 facilitates cytochrome c oxidase biogenesis as thiol-reductase for copper metallochaperones in mitochondria.

open access: yes, 2020
The mitochondrial cytochrome c oxidase, the terminal enzyme of the respiratory chain, contains heme and copper centers for electron transfer. The conserved COX2 subunit contains the CuA site, a binuclear copper center.
Aich, A.   +11 more
core   +2 more sources

Protein import into the endosymbiotic organelles of apicomplexan parasites [PDF]

open access: yes, 2018
The organelles of endosymbiotic origin, plastids, and mitochondria, evolved through the serial acquisition of endosymbionts by a host cell. These events were accompanied by gene transfer from the symbionts to the host, resulting in most of the organellar
Fellows, Justin   +3 more
core   +1 more source

Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB. [PDF]

open access: yes, 2020
NifB is a radical S-adenosyl-L-methionine (SAM) enzyme that is essential for nitrogenase cofactor assembly. Previously, a nitrogen ligand was shown to be involved in coupling a pair of [Fe4S4] clusters (designated K1 and K2) concomitant with carbide ...
Britt, R David   +7 more
core   +1 more source

Protein Targeting to the Albino3 Insertase

open access: yesThe FASEB Journal, 2010
The chloroplast thylakoid membrane is the site of photosynthetic light capture and oxygenic electron transport. Nuclear encoded light harvesting chlorophyll‐binding proteins (LHCPs), which bind chlorophyll a/b, provide much of the light absorbing capacity in plants.
Jennifer D Rogers   +6 more
openaire   +1 more source

The β-barrel membrane protein insertase machinery from Gram-negative bacteria [PDF]

open access: yesCurrent Opinion in Structural Biology, 2015
The outer membranes (OM) of Gram-negative bacteria contain a host of β-barrel outer membrane proteins (OMPs) which serve many functions for cell survival and virulence. The biogenesis of these OMPs is mediated by the β-barrel assembly machinery (BAM) complex which is composed of five components including the essential core component called BamA that ...
Nicholas, Noinaj   +2 more
openaire   +2 more sources

High-throughput screening of BAM inhibitors in native membrane environment

open access: yesNature Communications, 2023
The outer membrane insertase of Gram-negative bacteria, BAM, is a key target for urgently needed novel antibiotics. Functional reconstitutions of BAM have so far been limited to synthetic membranes and with low throughput capacity for inhibitor screening.
Parthasarathi Rath   +10 more
doaj   +1 more source

Structural basis for membrane insertion by the human ER membrane protein complex [PDF]

open access: yes, 2020
A defining step in the biogenesis of a membrane protein is the insertion of its hydrophobic transmembrane helices into the lipid bilayer. The nine-subunit endoplasmic reticulum (ER) membrane protein complex (EMC) is a conserved co- and posttranslational ...
Hazu, Masami   +5 more
core  

Monitoring Backbone Hydrogen-Bond Formation in β-Barrel Membrane Protein Folding [PDF]

open access: yes, 2016
β-barrel membrane proteins are key components of the outer membrane of bacteria, mitochondria and chloroplasts. Their three-dimensional structure is defined by a network of backbone hydrogen bonds between adjacent β-strands.
Hiller, Sebastian   +4 more
core   +1 more source

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