“Ribosomal L28e protein family”的意思、由来-开放百科全书

Ribosomal L28e protein family is a family of evolutionarily related proteins.

Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites.^[1]^[2] About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits.

Many of ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome.^[2]^[3]

Examples

References

1. ^{{cite journal | vauthors = Ramakrishnan V, Moore PB | title = Atomic structures at last: the ribosome in 2000 | journal = Curr. Opin. Struct. Biol. | volume = 11 | issue = 2 | pages = 144–54 | date = April 2001 | pmid = 11297922 | doi = 10.1016/s0959-440x(00)00184-6 }}
2. ^¹{{cite journal | vauthors = Maguire BA, Zimmermann RA | title = The ribosome in focus | journal = Cell | volume = 104 | issue = 6 | pages = 813–6 | date = March 2001 | pmid = 11290319 | doi = 10.1016/s0092-8674(01)00278-1 }}
3. ^{{cite journal | vauthors = Chandra Sanyal S, Liljas A | title = The end of the beginning: structural studies of ribosomal proteins | journal = Curr. Opin. Struct. Biol. | volume = 10 | issue = 6 | pages = 633–6 | date = December 2000 | pmid = 11114498 | doi = 10.1016/S0959-440X(00)00143-3 }}
4. ^{{cite journal | vauthors = Kuwano Y, Olvera J, Wool IG | title = The primary structure of rat ribosomal protein L38 | journal = Biochem. Biophys. Res. Commun. | volume = 175 | issue = 2 | pages = 551–5 | date = March 1991 | pmid = 1840484 | doi = 10.1016/0006-291x(91)91600-h }}
5. ^{{cite journal | vauthors = Wool IG, Chan YL, Paz V, Olvera J | title = The primary structure of rat ribosomal proteins: the amino acid sequences of L27a and L28 and corrections in the sequences of S4 and S12 | journal = Biochim. Biophys. Acta | volume = 1050 | issue = 1-3 | pages = 69–73 | date = August 1990 | pmid = 2207170 | doi = 10.1016/0167-4781(90)90143-p }}