Cell Organelles Involved in Protein Synthesis;
what cell organelle synthesizes proteins? | Yahoo Answers
N2 - During the development of pseudopodial spermatozoa of the nematode, Caenorhabditis elegans, protein synthesis stops before differentiation is completed. Colloidal gold conjugates of monoclonal antibody SP56, which binds to the surface of spermatozoa, and TR20, which recognizes the major sperm cytoplasmic protein (MSP), were used to label thin sections of testes embedded in Lowicryl K4M in order to follow polypeptides from their synthesis early in spermatogenesis to their segregation to specific compartments of the mature cell. Both antigens are synthesized in primary spermatocytes and are assembled into a unique double organelle, the fibrous body membranous organelle (FB-MO) complex. However, the antigens are localized in different regions of this FB-MO complex. As described in detail, the assembly of proteins into the FB-MO complex allows both membrane and cytoplasmic components to be concentrated in the spermatids after meiosis. Then, the stepwise disassembly of this transient structure ensures delivery of each component to its final destination in the mature spermatozoan: MSP filaments in the fibrous body depolymerize, releasing MSP into the cytoplasm and the membranous organelles fuse with the plasma membrane, delivering SP56 antigen to the surface.
Immunofluorescence assays on parasites expressing the ApicEFG-GFP episome in conjunction with ACP as an apicoplast marker reveal that PFF0115c is indeed localised to the P. falciparum apicoplast (). Both ACP antibody labelling and ApicEFG-GFP fluorescence revealed a dot-like organelle in the parasite, characteristic of the apicoplast in ring stage parasites during the asexual cycle . These data confirm that the gene annotated as PFF0115c is a nucleus-encoded EF-G protein targeted to the P. falciparum apicoplast.
17/01/2009 · which cell organelle synthesizes proteins
(monoclonal antibody omics) develops monoclonal antibodies for thousands of expressed proteins in a proteome (biological sample). A protein sample (for example, plasma; or a tissue; or a cellular organelle) is processed to produce protein and peptide fractions as immunogens. A set of proprietary mouse monoclonal antibody technologies is employed to produce 10,000-100,000 individual mouse hybridomas to cover a significant portion (typically 30-70%) of the proteome. Thus produced libraries have broad applications in differential proteomics and reagent development.
AB - During the development of pseudopodial spermatozoa of the nematode, Caenorhabditis elegans, protein synthesis stops before differentiation is completed. Colloidal gold conjugates of monoclonal antibody SP56, which binds to the surface of spermatozoa, and TR20, which recognizes the major sperm cytoplasmic protein (MSP), were used to label thin sections of testes embedded in Lowicryl K4M in order to follow polypeptides from their synthesis early in spermatogenesis to their segregation to specific compartments of the mature cell. Both antigens are synthesized in primary spermatocytes and are assembled into a unique double organelle, the fibrous body membranous organelle (FB-MO) complex. However, the antigens are localized in different regions of this FB-MO complex. As described in detail, the assembly of proteins into the FB-MO complex allows both membrane and cytoplasmic components to be concentrated in the spermatids after meiosis. Then, the stepwise disassembly of this transient structure ensures delivery of each component to its final destination in the mature spermatozoan: MSP filaments in the fibrous body depolymerize, releasing MSP into the cytoplasm and the membranous organelles fuse with the plasma membrane, delivering SP56 antigen to the surface.
What cell organelle synthesizes proteins
The identification of two nucleus-encoded, organelle localised EF-Gs that could be the target of the same inhibitor presents unique opportunities for the investigation of the effects of organelle specific drugs and in the development of novel anti-malarials. For almost all anti-bacterial compounds currently in use, the target (or predicted target) is encoded on the genome of at least one of the organelles , , making them refractory to genetic manipulation and difficult to investigate. The presence of nucleus-encoded EF-Gs in both the mitochondrion and apicoplast provides the opportunity to use known bacterial resistance mutations to dissect the effects of specifically blocking protein synthesis in each organelle. It also presents the possibility of developing novel compounds that target EF-G in both organelles, thereby yielding a single anti-malarial compound that could have all the advantages of a multi-drug therapy in terms of avoiding drug resistance.
Two candidate EF-G proteins that may be fusidic acid targets were identified and localised (–). Bioinformatic analysis is consistent with these proteins having been introduced as endosymbiont-derived genes that are now located in the parasite nucleus. One EF-G is localised in the parasite mitochondrion, and the second is localised to the relict plastid or apicoplast (,). Comparisons between primary protein structure of the apicoplast and mitochondrial EF-Gs and sensitive bacterial EF-G proteins suggests that the apicoplast localised EF-G is sensitive to fusidic acid while the mitochondrial EF-G carries a single amino acid residue that confers a weak resistance phenotype in S. aureus (,). Although this finding implies that the P. falciparum mitochondrial EF-G may be resistant to fusidic acid, differences between the bacterial and Plasmodium mitochondrial EF-Gs at other conserved positions makes it difficult to draw specific conclusions about the sensitivity of the P. falciparum mitochondrial EF-G to fusidic acid from this single amino acid change without further investigation. A further possibility is that fusidic acid acts by targeting a mechanism unrelated to organellar protein synthesis, but the two EF-Gs identified here represent the most likely targets and require further investigation.
Section 5.4 Organelles of the Eukaryotic Cell
membrane and organelle proteins and ..
Organelle Protein Synthesis.
where are the proteins synthesized in the cell
where proteins are ..
Membrane phospholipid synthesis and endoplasmic …
Organelles Working Together
Bio Resource Biotech | Antibody | Proteins - Scribd
The mechanism for transporting newly synthesized proteins is highly conserved from bacteria to mammals. A key difference, however, is that bacteria translocate the proteins directly across the plasma membrane to the outside world, whereas eukaryotic cells translocate them into a specialized intracellular organelle, the endoplasmic reticulum. Newly synthesized proteins are conveyed from the endoplasmic reticulum to the cell surface via a series of carrier vesicles. It is therefore useful to consider prokaryotic and eukaryotic protein secretion separately.
30/12/2017 · Bio Resource Biotech
We have analyzed DNA PolIB mutants and observed a 30% reduction in mtDNA copy number and changes in respiration activity (Cupp and Nielsen 2013). The PolIB homozygous mutant has a large decrease in mitochondria size and a simultaneous significant increase in the number of mitochondria per cell. However, no effects on chloroplast size or number were observed. We are currently analyzing the DNA PolIA mutants to determine the effect of the mutation on genome copy number and organelle structure, and on respiration and photosynthesis activity. This protein is dual-localized under specific conditions (Christensen et al. 2005), but under other conditions PolIA is preferentially localized to chloroplasts (Elo et al. 2003, see Preliminary Studies), and it may play a more predominant role in chloroplasts and have different functions in each organelle.
Protein & Peptide Sample Fractionation, Organelle ..
Recombination-dependent replication (RDR). With the growing evidence that RDR may be a major mechanism for DNA replication in one or both plant organelles, this infers that one or more recombinases may be involved to facilitate DNA synthesis. Three bacterial RecA orthologs have been identified as RecA1, RecA2, and RecA3 in the Arabidopsis genome (Khazi et al. 2003; Shedge et al. 2007). RecA1 is localized to chloroplasts, RecA2 is dual-localized, and RecA3 is found in mitochondria. As mentioned above, RecA1 is co-expressed in Arabidopsis along with DNA PolIA, supporting the possibility that these two proteins function together. RecA1 and RecA3 are coexpressed with different genes involved in development (ATTED database). No coexpression data is available for RecA2. Shedge et al. (2007) reported that RecA1 is essential in Arabidopsis, as homozygous mutants are not viable. If this protein only functioned in repair it would be expected that mutants would still be viable but unable to repair DNA damage, which suggests that RecA1 may play a critical role in ctDNA replication, and not just in DNA repair. In support of this, the involvement of RecA1 in maintenance of ctDNA integrity has been reported (Rowan et al. 2010). Mutants in RecA1 resulted in altered ctDNA structure and reduced ctDNA levels, along with an increase in single-stranded regions of ctDNA. Parallel functions for RecA2 and RecA3 may contribute to mtDNA replication and genome maintenance. Strand invasion catalyzed by one of the RecA homologs followed by extension of new DNA synthesis by one or both of the organellar DNA polymerases may be directly involved in organelle genome replication.
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