Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients
Membrane protein biogenesis in the endoplasmic reticulum (ER) is complex and failure-prone. The ER membrane protein complex (EMC), comprising eight conserved subunits, has emerged as a central player in this process. Yet, we have limited understanding of
Lakshmi E Miller-Vedam +13 more
doaj +1 more source
YidC/Alb3/Oxa1 Family of Insertases [PDF]
The YidC/Alb3/Oxa1 family functions in the insertion and folding of proteins in the bacterial cytoplasmic membrane, the chloroplast thylakoid membrane, and the mitochondrial inner membrane. All members share a conserved region composed of five transmembrane regions.
Seth W, Hennon +3 more
openaire +2 more sources
Localization of proteins involved in the biogenesis and repair of the photosynthetic apparatus to thylakoid subdomains in Arabidopsis. [PDF]
Abstract Thylakoid membranes in chloroplasts and cyanobacteria harbor the multisubunit protein complexes that catalyze the light reactions of photosynthesis. In plant chloroplasts, the thylakoid membrane system comprises a highly organized network with several subcompartments that differ in composition and morphology: grana stacks, unstacked stromal ...
Chotewutmontri P, Barkan A.
europepmc +2 more sources
Nitrogenase Fe protein: A molybdate/homocitrate insertase [PDF]
The Fe protein is indispensable for nitrogenase catalysis and biosynthesis. However, its function in iron-molybdenum cofactor (FeMoco) biosynthesis has not been clearly defined. Here we show that the Fe protein can act as a Mo/homocitrate insertase that mobilizes Mo/homocitrate for the maturation of FeMoco precursor on NifEN. Further, we establish that
Yilin, Hu +6 more
openaire +2 more sources
A common evolutionary origin reveals fundamental principles of protein insertases
Membrane proteins require protein machineries to insert their hydrophobic transmembrane domains (TMDs) into the lipid bilayer. A functional analysis of protein insertases in this issue of PLOS Biology reveals that the fundamental mechanism of membrane protein insertion is universally conserved.
Vögtle, Friederike Nora +2 more
openaire +5 more sources
Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts [PDF]
Members of the YidC/Oxa1/Alb3 protein family facilitate the insertion, folding and assembly of proteins of the inner membranes of bacteria and mitochondria and the thylakoid membrane of plastids.
Funes, Soledad +4 more
core +1 more source
The membrane insertases YidC-Oxa1-Alb3 provide a simple cellular system that catalyzes the transmembrane topology of newly synthesized membrane proteins. The insertases are composed of a single protein with 5 to 6 transmembrane (TM) helices that contact hydrophobic segments of the substrate proteins.
Dalbey, Ross E. +3 more
openaire +2 more sources
Human mitochondria express a genome that encodes thirteen core subunits of the oxidative phosphorylation system (OXPHOS). These proteins insert into the inner membrane co-translationally. Therefore, mitochondrial ribosomes engage with the OXA1L-insertase
Sven Dennerlein +12 more
doaj +1 more source
Analysis of the Sam50 translocase of excavate organisms supports evolution of divergent organelles from a common endosymbiotic event [PDF]
As free-living organisms the ancestors of mitochondria and plastids encoded complete genomes, proteomes and metabolomes. As these symbionts became organelles all these aspects were reduced – genomes have degenerated with the host nucleus now encoding the
Bradley +30 more
core +3 more sources
Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC [PDF]
Protein secretion and membrane insertion occur through the ubiquitous Sec machinery. In this system, insertion involves the targeting of translating ribosomes via the signal recognition particle and its cognate receptor to the SecY (bacteria and archaea)/
Alvira-de-Celis, Sara +10 more
core +4 more sources

