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The lac repressor (LacI) is a DNA-binding protein that inhibits the expression of genes coding for proteins involved in the metabolism of lactose in bacteria. These genes are repressed when lactose is not available to the cell, ensuring that the bacterium only invests energy in the production of machinery necessary for uptake and utilization of lactose when lactose is present. When lactose becomes available, it is firstly converted into allolactose by β-Galactosidase (lacZ) in bacteria. The DNA binding ability of lac repressor bound with allolactose is inhibited due to allosteric regulation, thereby genes coding for proteins involved in lactose uptake and utilization can be expressed.
In biology, an effector is a general term that can refer to several types of molecules or cells depending on the context:
Ribosome display is a technique used to perform in vitro protein evolution to create proteins that can bind to a desired ligand. The process results in translated proteins that are associated with their mRNA progenitor which is used, as a complex, to bind to an immobilized ligand in a selection step. The mRNA-protein hybrids that bind well are then reverse transcribed to cDNA and their sequence amplified via PCR. The result is a nucleotide sequence that can be used to create tightly binding proteins.
The start codon is the first codon of a messenger RNA (mRNA) transcript translated by a ribosome. The start codon always codes for methionine in eukaryotes and archaea and a N-formylmethionine (fMet) in bacteria, mitochondria and plastids.
Bacterial translation is the process by which messenger RNA is translated into proteins in bacteria.
Eukaryotic translation is the biological process by which messenger RNA is translated into proteins in eukaryotes. It consists of four phases: initiation, elongation, termination, and recapping.
EF-Tu is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome. It is a G-protein, and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome. As a reflection of its crucial role in translation, EF-Tu is one of the most abundant and highly conserved proteins in prokaryotes. It is found in eukaryotic mitochondria as TUFM.
A bacterial initiation factor (IF) is a protein that stabilizes the initiation complex for polypeptide translation.
The PreQ1-I riboswitch is a cis-acting element identified in bacteria which regulates expression of genes involved in biosynthesis of the nucleoside queuosine (Q) from GTP. PreQ1 (pre-queuosine1) is an intermediate in the queuosine pathway, and preQ1 riboswitch, as a type of riboswitch, is an RNA element that binds preQ1. The preQ1 riboswitch is distinguished by its unusually small aptamer, compared to other riboswitches. Its atomic-resolution three-dimensional structure has been determined, with the PDB ID 2L1V.
A ribosome binding site, or ribosomal binding site (RBS), is a sequence of nucleotides upstream of the start codon of an mRNA transcript that is responsible for the recruitment of a ribosome during the initiation of translation. Mostly, RBS refers to bacterial sequences, although internal ribosome entry sites (IRES) have been described in mRNAs of eukaryotic cells or viruses that infect eukaryotes. Ribosome recruitment in eukaryotes is generally mediated by the 5' cap present on eukaryotic mRNAs.
The prokaryotic small ribosomal subunit, or 30S subunit, is the smaller subunit of the 70S ribosome found in prokaryotes. It is a complex of the 16S ribosomal RNA (rRNA) and 19 proteins. This complex is implicated in the binding of transfer RNA to messenger RNA (mRNA). The small subunit is responsible for the binding and the reading of the mRNA during translation. The small subunit, both the rRNA and its proteins, complexes with the large 50S subunit to form the 70S prokaryotic ribosome in prokaryotic cells. This 70S ribosome is then used to translate mRNA into proteins.
The 23S rRNA is a 2,904 nucleotide long component of the large subunit (50S) of the bacterial/archean ribosome and makes up the peptidyl transferase center (PTC). The 23S rRNA is divided into six secondary structural domains titled I-VI, with the corresponding 5S rRNA being considered domain VII. The ribosomal peptidyl transferase activity resides in domain V of this rRNA, which is also the most common binding site for antibiotics that inhibit translation, making it a target for ribosomal engineering. A well-known member of this antibiotic class, chloramphenicol, acts by inhibiting peptide bond formation, with recent 3D-structural studies showing two different binding sites depending on the species of ribosome. Numerous mutations in domains of the 23S rRNA with Peptidyl transferase activity have resulted in antibiotic resistance. 23S rRNA genes typically have higher sequence variations, including insertions and/or deletions, compared to other rRNAs.
Eukaryotic translation initiation factor 4E, also known as eIF4E, is a protein that in humans is encoded by the EIF4E gene.
EF-G is a prokaryotic elongation factor involved in protein translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.
A protein synthesis inhibitor is a compound that stops or slows the growth or proliferation of cells by disrupting the processes that lead directly to the generation of new proteins.
The A-site of a ribosome is a binding site for charged t-RNA molecules during protein synthesis. One of three such binding sites, the A-site is the first location the t-RNA binds during the protein synthesis process, the other two sites being P-site (peptidyl) and E-site (exit).
The P-site is the second binding site for tRNA in the ribosome. The other two sites are the A-site (aminoacyl), which is the first binding site in the ribosome, and the E-site (exit), the third. During protein translation, the P-site holds the tRNA which is linked to the growing polypeptide chain. When a stop codon is reached, the peptidyl-tRNA bond of the tRNA located in the P-site is cleaved releasing the newly synthesized protein. During the translocation step of the elongation phase, the mRNA is advanced by one codon, coupled to movement of the tRNAs from the ribosomal A to P and P to E sites, catalyzed by elongation factor EF-G.
EF-P is an essential protein that in bacteria stimulates the formation of the first peptide bonds in protein synthesis. Studies show that EF-P prevents ribosomes from stalling during the synthesis of proteins containing consecutive prolines. EF-P binds to a site located between the binding site for the peptidyl tRNA and the exiting tRNA. It spans both ribosomal subunits with its amino-terminal domain positioned adjacent to the aminoacyl acceptor stem and its carboxyl-terminal domain positioned next to the anticodon stem-loop of the P site-bound initiator tRNA. The EF-P protein shape and size is very similar to a tRNA and interacts with the ribosome via the exit “E” site on the 30S subunit and the peptidyl-transferase center (PTC) of the 50S subunit. EF-P is a translation aspect of an unknown function, therefore It probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Woese's dogma is a principle of evolutionary biology first put forth by biophysicist Carl Woese in 1977. It states that the evolution of ribosomal RNA was a necessary precursor to the evolution of modern life forms. This led to the advancement of the phylogenetic tree of life consisting of three domains rather than the previously accepted two. While the existence of Eukarya and Prokarya were already accepted, Woese was responsible for the distinction between Bacteria and Archaea. Despite initial criticism and controversy surrounding his claims, Woese's three domain system, based on his work regarding the role of rRNA in the evolution of modern life, has become widely accepted.
Yoshito Kaziro was a Japanese biochemical and medical scientist who performed research on the effects and mechanisms of ATP and GTP driven conformational changes in enzymes and intracellular signaling pathways for over 50 years. He is well-known for his research on various signal transduction pathways involving GTP-binding proteins and the mechanism for biotin dependent carboxylation reactions of Coenzyme A (CoA) proteins.
References
- ↑ Chen, C.; Stevens, B.; Kaur, J.; Smilansky, Z.; Cooperman, B. S.; Goldman, Y. E. (2011-10-03). "Allosteric vs. spontaneous exit-site (E-site) tRNA dissociation early in protein synthesis". Proceedings of the National Academy of Sciences. 108 (41): 16980–16985. Bibcode:2011PNAS..10816980C. doi: 10.1073/pnas.1106999108 . ISSN 0027-8424. PMC 3193197 . PMID 21969541.
- ↑ Kirillov, S., Makarov, E., & Semenkov, Y. (1983). Quantitative study of interaction of deacylated tRNA with Escherichia coli ribosomes. FEBS Letters, 157(1), 91-94. doi : 10.1016/0014-5793(83)81122-3
- ↑ dx.doi.org. doi:10.17658/issn.2058-5462/issue-23/efisher/p1 http://dx.doi.org/10.17658/issn.2058-5462/issue-23/efisher/p1 . Retrieved 2024-01-26.
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- Sergiev, Petr V.; Lesnyak, Dmitry V.; Kiparisov, Sergey V.; Burakovsky, Dmitry E.; Leonov, Andrei A.; Bogdanov, Alexey A.; Brimacombe, Richard; Dontsova, Olga A. (2005). "Function of the ribosomal E-site: a mutagenesis study". Nucleic Acids Research. 33 (18): 6048–6056. doi:10.1093/nar/gki910. ISSN 0305-1048. PMC 1266066 . PMID 16243787.
- Chen, Chunlai; Stevens, Benjamin; Kaur, Jaskiran; Smilansky, Zeev; Cooperman, Barry S.; Goldman, Yale E. (2011-10-11). "Allosteric vs. spontaneous exit-site (E-site) tRNA dissociation early in protein synthesis". Proceedings of the National Academy of Sciences. 108 (41): 16980–16985. Bibcode:2011PNAS..10816980C. doi: 10.1073/pnas.1106999108 . ISSN 0027-8424. PMC 3193197 . PMID 21969541.
- Molecular Biology of the Gene, 7th Edition, James D. Watson, Tania A. Baker,Stephen P. Bell,Alexander Gann, Michael Levine,Richard Losick, ©2014 Pearson
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