Ribosomes (/ˈraɪbəzoʊm, -soʊm/) are macromolecular biological machines found within all cells that perform messenger RNA translation. Ribosomes link amino acids together in the order specified by the codons of messenger RNA molecules to form polypeptide chains. Ribosomes consist of two major components: the small and large ribosomal subunits. Each subunit consists of one or more ribosomal RNA molecules and many ribosomal proteins (r-proteins). The ribosomes and associated molecules are also known as the translational apparatus.
>>>PUT SHARE BUTTONS HERE<<<
In this Dossier
Ribosomal protein in the context of Ribosomal RNA
Ribosomal ribonucleic acid (rRNA) is a type of non-coding RNA which is the primary component of ribosomes, essential to all cells. rRNA is a ribozyme which carries out protein synthesis in ribosomes. Ribosomal RNA is transcribed from ribosomal DNA (rDNA) and then bound to ribosomal proteins to form small and large ribosome subunits. rRNA is the physical and mechanical factor of the ribosome that forces transfer RNA (tRNA) and messenger RNA (mRNA) to process and translate the latter into proteins. Ribosomal RNA is the predominant form of RNA found in most cells; it makes up about 80% of cellular RNA despite never being translated into proteins itself. Ribosomes are composed of approximately 60% rRNA and 40% ribosomal proteins, though this ratio differs between prokaryotes and eukaryotes.
Ribosomal protein in the context of Nuclear pore
The nuclear pore complex (NPC), is a large protein complex giving rise to the nuclear pore. A great number of nuclear pores are studded throughout the nuclear envelope that surrounds the eukaryote cell nucleus. The pores enable the nuclear transport of macromolecules between the nucleoplasm of the nucleus and the cytoplasm of the cell. Small molecules can easily diffuse through the pores. Nuclear transport includes the transportation of RNA and ribosomal proteins from the nucleus to the cytoplasm, and the transport of proteins (such as DNA polymerase and lamins), carbohydrates, signaling molecules, and lipids into the nucleus. Each nuclear pore complex can actively mediate up to 1000 translocations per second.
The nuclear pore complex consists predominantly of a family of proteins known as nucleoporins (Nups). Each pore complex in the human cell nucleus is composed of about 1,000 individual protein molecules, from an evolutionarily conserved set of 35 distinct nucleoporins. The conserved sequences that code for nucleoporins regulate molecular transport through the nuclear pore. Nucleoporin-mediated transport does not entail direct energy expenditure but instead relies on concentration gradients associated with the RAN cycle (Ras-related nuclear protein cycle). In 2022 around 90% of the structure of the human NPC was elucidated in an open and a closed conformation, and published in a special issue of Science, featured on the cover. In 2024 the structure of the nuclear basket was solved, finalising the completion of the structure of the nuclear pore complex.