These organisms were classified in the class Actinosporea, until careful experimentation supported by analysis of the 18S Ribosomal Subunit RNA sequence in the early 1990s allowed matching of several actinosporeans with their myxosporean equivalent.
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit.
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.
EIF4E3 belongs to the EIF4E family of translational initiation factors that interact with the 5-prime cap structure of mRNA and recruit mRNA to the ribosome.
This hypothesis was originally proposed by James A. Lake and colleagues in 1984 based on the discovery that the shapes of ribosomes in the Crenarcaeota and eukaryotes are more similar to each other than to either bacteria or the second major kingdom of archaea, the Euryarchaeota.
Similar to the hairpin ribozyme, the HDV ribosome has reactions that is characterized by acid-base catalysis.
The insulin-like growth factor II (IGF-II) internal ribosome entry site IRES is found in the 5' UTR of IGF-II leader 2 mRNA.
It is bacteriostatic and acts by inhibiting bacterial protein synthesis via binding with the 50S subunit of the ribosome.
After assembly of these primary binding proteins, S5, S6, S9, S12, S13, S16, S18, and S19 bind to the growing ribosome.
The ribosome recycling factor was discovered in the early 1970s by the work of Akira Kaji and Akikazu Hiroshima at the University of Pennsylvania.
This sequence is recognised by a cytosolic protein, SRP (Signal Recognition Particle), which stops the translation and aids in the transport of the mRNA-ribosome complex to an SRP receptor found in the membrane of the endoplasmic reticulum.
SENP3 is associated and regulated by B23/nucleophosmin/NPM1 and involved in the regulation of ribosome biogenesis.
SIRT7 is active in the nucleolus, a compartment of the nucleus reserved for the assembly of ribosomes.
This region has been shown to mediate internal ribosome entry in cells derived from brain, heart, and skeletal muscle; tissues known to express mRNA species.