Some sequences are similar to those proven to be targets for effective intervention in other protozoan parasites, and include not only proteases, antioxidant enzymes, and heat shock proteins, but also those associated with relict plastids, such as acetyl-CoA carboxylase and methyl erythrithol phosphate pathway components, and those involved in glycan assembly, protein folding/secretion, and parasite-host interactions. (biomedcentral.com)
TRiC, the eukaryotic chaperonin, is composed of two rings of eight different though related subunits, each thought to be represented once per eight-membered ring. (wikipedia.org)
Peptides2
Some bacteria use multiple copies of this chaperonin, probably for different peptides. (wikipedia.org)
From the identified 2938 proteins and 7503 unique peptides, we characterized N-terminal methionine excision, co- and posttranslational Nα acetylation, protein maturation, and proteolytic processing of proteins in human platelets. (ashpublications.org)
Substrates6
GroEL is a double-ring 14mer with a greasy hydrophobic patch at its opening and can accommodate the native folding of substrates 15-60 kDa in size. (wikipedia.org)
TRiC was originally thought to fold only the cytoskeletal proteins actin and tubulin but is now known to fold dozens of substrates. (wikipedia.org)
Group II chaperonins are not thought to utilize a GroES-type cofactor to fold their substrates. (wikipedia.org)
They instead contain a "built-in" lid that closes in an ATP-dependent manner to encapsulate its substrates, a process that is required for optimal protein folding activity. (wikipedia.org)
Recent structural data suggest an effective size limit for the TRiC folding chamber of ∼70 kDa, but numerous chaperonin substrates are substantially larger. (cipsm.de)
System-wide identification of metalloproteinase and other proteinase substrates and their respective cleavage sites suggests novel mechanisms of the effect of proteases on protein activity and platelet function during storage. (ashpublications.org)
Phage1
A Group I chaperonin gp146 from phage EL does not use a lid, and its donut interface is more similar to Group II. (wikipedia.org)
Cytosol1
Chloroplast-located proteins which are encoded by the nuclear genome have to be imported from the cytosol into the organelle in a post-translational manner. (cipsm.de)
Subunits4
Each ring is composed of either 7, 8 or 9 subunits depending on the organism in which the chaperonin is found. (wikipedia.org)
Methanococcus maripaludis chaperonin (Mm cpn) is composed of sixteen identical subunits (eight per ring). (wikipedia.org)
The BCKD enzyme is a multimeric enzyme complex with four components, branched-chain keto acid decarboxylase alpha and beta subunits (E1 α and E1 β ), dihydrolipoyl transacylase (E2) subunit, and dihydrolipoamide dehydrogenase (E3) subunit. (nature.com)
Newly made proteins usually must fold from a linear chain of amino acids into a three-dimensional tertiary structure. (wikipedia.org)
The PCM is an ordered lattice that anchors a large number of microtubule (MT)-associated proteins, many of which bear putative coiled-coil domains, a tertiary structure known to facilitate protein-protein interactions [ 4 ]. (biomedcentral.com)
Members of the Alb3/Oxa1/YidC protein family function as insertases in chloroplasts, mitochondria, and bacteria. (cipsm.de)
The vesicle-inducing protein in plastids 1 (Vipp1) is an essential component for thylakoid biogenesis in cyanobacteria and chloroplasts. (cipsm.de)
Genome1
The gene set of the last common ancestor of the crown group consists of 3,413 KOGs and largely includes proteins involved in genome replication and expression, and central metabolism. (biomedcentral.com)
Apical1
A close relationship with the Apicomplexa was initially proposed based on the ultrastructural analysis of the zoospore, which revealed the presence of organelles resembling an apical complex [ 7 ]. (biomedcentral.com)
Interactions2
The energy to fold proteins is supplied by non-covalent interactions between the amino acid side chains of each protein, and by solvent effects. (wikipedia.org)
According to recent analyses by different experimental techniques, GroEL-bound substrate proteins populate an ensemble of compact and locally expanded states that lack stable tertiary interactions. (wikipedia.org)
Reaction1
Chaperonins undergo large conformational changes during a folding reaction as a function of the enzymatic hydrolysis of ATP as well as binding of substrate proteins and cochaperonins, such as GroES. (wikipedia.org)
Targets2
It provides a very informative, albeit preliminary, glimpse into the expression of genes encoding functionally relevant proteins as potential targets for chemotherapy, and evidence for the presence of a relict plastid. (biomedcentral.com)
Enthrallingly, HTLV-1 Tax expression also targets the functions of the centrosome, and this event is correlated with centrosome amplification, aneuploidy and transformation. (biomedcentral.com)
Bacteria1
Due to independent gene duplications, all organisms possess two isoforms, Oxa1 and Oxa2 except gram-negative bacteria, which encode only for one YidC-like protein. (cipsm.de)
Particles2
Immunogold uses the power of antibodies and electron dense, colloidal gold particles while METTEM uses metallothionein (MT), a metal-binding protein as a clonable tag. (bvsalud.org)
In all living cells, protein synthesis occurs on ribonucleoprotein particles called ribosomes. (cipsm.de)
Large2
The GroEL/GroES complex in E. coli is a Group I chaperonin and the best characterized large (~ 1 MDa) chaperonin complex. (wikipedia.org)
The sHsps investigated to date mostly form large, oligomeric complexes. (cipsm.de)
Pathway1
GroEL/GroES may not be able to undo protein aggregates, but kinetically it competes in the pathway of misfolding and aggregation, thereby preventing aggregate formation. (wikipedia.org)
Functional2
Most proteins spontaneously fold into their most stable three-dimensional conformation, which is usually also their functional conformation, but occasionally proteins mis-fold. (wikipedia.org)
The cpn10 and cpn60 oligomers also require Mg2+-ATP in order to interact to form a functional complex. (wikipedia.org)
Viruses3
Specially, when studying viruses in cells, methodologies for labeling proteins and other macromolecules are important tools to correlate morphology with function. (bvsalud.org)
Several viruses including retroviruses such as, Foamy Virus, HIV-1, JSRV, M-PMV and HTLV-1 have been shown to hamper centrosome functions for their own profit, but the outcomes are very different. (biomedcentral.com)
Foamy viruses, HIV-1, JSRV, M-PMV and HTLV-1 use the cellular machinery to traffic towards the centrosome during early and/or late stages of the infection. (biomedcentral.com)
Expression1
A significant dose-dependent reduction of the expression levels of Gc and N viral proteins was also measured. (bvsalud.org)
Immunofluorescence and confocal microscopy showed that ASA protects the Golgi complex from the characteristic BUNV-induced fragmentation in Vero cells. (bvsalud.org)
Human2
TAILS proteomics identified 2938 human platelet proteins, pervasive proteolytic processing, and precise proteolytic cleavage sites in stored platelets. (ashpublications.org)
We also identified for the first time 10 proteins previously classified by the Human Proteome Organization as "missing" in the human proteome. (ashpublications.org)
Translation1
The approximately 40% of KOGs that are represented in six or seven species are enriched in proteins responsible for housekeeping functions, particularly translation and RNA processing. (biomedcentral.com)
Activity1
Four drugs, OSW-1, U18666A, hydroxypropyl-ß-cyclodextrin (HßCD) and phytol, showed in vitro antiviral activity against HCoV-229E and SARS-CoV-2. (bvsalud.org)
Centrosomes were first described at the end of the 19th century by Theodor Boveri who had also the intuition of their central role in cell life [ 1 ]. (biomedcentral.com)
Case1
Orthology and paralogy are intimately linked because, if a duplication (or a series of duplications) occurs after the speciation event that separated the compared species, orthology becomes a relationship between sets of paralogs, rather than individual genes (in which case, such genes are called co-orthologs). (biomedcentral.com)
Functions1
In addition HIV-1 Vpr protein alters the cell-cycle regulation by hijacking centrosome functions. (biomedcentral.com)
Family1
The RuBisCO subunit binding protein is a member of this family. (wikipedia.org)