(redirected from Ribosomal proteins)
Also found in: Dictionary, Thesaurus, Medical.


see cellcell,
in biology, the unit of structure and function of which all plants and animals are composed. The cell is the smallest unit in the living organism that is capable of integrating the essential life processes. There are many unicellular organisms, e.g.
..... Click the link for more information.
; nucleic acidnucleic acid,
any of a group of organic substances found in the chromosomes of living cells and viruses that play a central role in the storage and replication of hereditary information and in the expression of this information through protein synthesis.
..... Click the link for more information.



an intracellular particle concerned with protein biosynthesis that is found in the cells of all living organisms (bacteria, plants, and animals); each cell contains thousands or tens of thousands of ribosomes. Ribosomes are close to spherical in shape, although their outlines are complex and cannot be described by a simple geometric figure.

Two major classes of ribosomes are distinguished: 70S and 80S. The 70S ribosome has a molecular weight of about 3 × 106, a diameter of about 200-300 angstroms (Å), and a sedimentation coefficient Ribosomeof about 70 Svedberg units. The larger, 80S, ribosome has a molecular weight of about 4–5 × 106, a maximum diameter reaching 400 Å, and a sedimentation coefficient of about 80 Svedberg units. Ribosomes of the 70S class are characteristic of prokaryotes—cells that do not have a structured nucleus—including bacteria, actinomycetes, and blue-green algae, as well as of the chloroplasts and mitochondria of higher organisms. Ribosomes of the 80S class are found in the cytoplasm of all eukaryotes—organisms that have a structured cell nucleus.

Chemically, ribosomes are nucleoproteins that consist of ribonucleic acid (RNA) and protein. Ribosomes of the 70S class consist of 60-65 percent RNA and 40-35 percent protein, while ribosomes of the 80S class consist of about 50 percent RNA and 50 percent protein. The general principle of the structural organization of ribosomes is that they are composed of two unequal subparticles, or subunits, to which a ribosome may dissociate (for example, upon a decrease in the concentration of Mg2+ ions in a medium) and reassociate according to the formula

70S ⇄ 50S + 30S 80S ⇄ 60S + 40S

The large subunit (50S or 60S) consists of a high-polymer molecule of ribosomal RNA that has a molecular weight of 1.1-1.8 × 106, a low-polymer molecule of ribosomal RNA that has a molecular weight of 40,000, and several tens of protein molecules. The small subunit (30S or 40S) consists of a molecule of ribosomal RNA that exhibits high polymerism and has a molecular weight of 0.6-0.7 × 106 and from 20 (in 30S subunits) to 40 (in 40S subunits) various protein molecules.

The high-polymer ribosomal RNA binds proteins into a single ribonucleoprotein particle. It is experimentally possible to unwind ribosomes—the unit becomes more friable and the RNA unwinds into a strand. During this process, all proteins remain attached to the particle. Under other conditions, the sequential cleavage of proteins from RNA may be achieved; this process is known as the separation of ribosomes. This separation is reversible and under suitable conditions proteins and RNA spontaneously reunite into a ribonucleoprotein, which forms the native structure of a ribosome; this process is known as the self-assembly of ribosomes. The self-assembly of previously synthesized RNA and proteins is also believed to form ribosomes in cells.

Ribosomes have several functions in the synthesis of proteins, including the specific binding and retention of the components of the system that synthesizes proteins; these components include messenger RNA (mRNA), aminoacyl-transfer RNA (aminoacyl-tRNA), peptidyl-tRNA, guanosine triphosphate (GTP), and the protein translation factors EF-T and EF-G. Ribosomes also have catalytic functions, including the formation of peptide bonds and the hydrolysis of GTP. They also assist in the mechanical displacement of substrates, for example, mRNA and tRNA, and in translocation.

The functions of catalysis and the retention of components are distributed between two ribosomal subunits. The small ribosomal subunit contains segments that bind mRNA and aminoacyl-tRNA; it apparently has no catalytic functions. The large subunit contains both a catalytic segment that catalyzes the formation of the peptide bond and a center that participates in the hydrolysis of GTP. During protein biosynthesis, the large subunit retains the growing protein chain in the form of pepti-dyl-tRNA. Each subunit may perform its functions independently of the other subunit. The function of translocation, however, can only be accomplished by the whole ribosome and not by the individual ribosomal subunits.


Spirin, A. S., and L. P. Gavrilova. Ribosoma, 2nd ed. Moscow, 1971.



(cell and molecular biology)
One of the small, complex particles composed of various proteins and three molecules of ribonucleic acid which synthesize proteins within the living cell.
References in periodicals archive ?
The 50 most expressed genes in velvet skin included genes belonging to the ribosomal protein and collagen families (Table II).
A new system for naming ribosomal proteins," Current Opinion in Structural Biology, vol.
siRNA knockdown of ribosomal protein gene RPL19 abrogates the aggressive phenotype of human prostate cancer.
In animals, ribosomal proteins have been widely used for phylogenetic analysis as they are highly conserved and offer useful comparisons between distant lineages.
The cfr gene and mutations in ribosomal proteins L4 or L22 were not detected in the study isolates.
S6K1-mediated phosphorylation of S6 was believed for quite a while to promote the translation of TOP mRNAs (5'-terminal oligopyrimidine mRNAs) that encode ribosomal proteins and translation factors, but some new evidence indicated that phosphorylation of S6 was not critical for TOP translation (Magnuson et al.
S6K-deficient mice with mutated versions of the S6 ribosomal protein have reduced [beta]-cell mass, hypoinsulinemia and glucose intolerance (53).
Differential transcript profiles, possibly relevant to rodent follicular cell tumor outcomes, were observed in rats exposed to PB and PTU, including genes involved in Wnt signaling and ribosomal protein expression.
These included eight different ribosomal proteins, represented by 10 individual clones, and a variety of protein kinases.
There's no convincing evidence that ribosomal RNA genes or genes for ribosomal proteins are transferred horizontally.
The discovery was interesting because mutations affecting one of the same ribosomal proteins in humans are associated with Diamond-Blackfan syndrome, a condition that causes a type of anemia specific to red blood cells.

Full browser ?