Description

IPR023442 is a Large ribosomal subunit protein eL24, conserved site.

<p>This entry represents a conserved sequence region found towards the N terminus of ribosomal protein eL24 (previously known as L24). It is also found in ribosomal protein eL24-like, an essential protein with similarity to Rpl24Ap and Rpl24Bp, which is associated with pre-60S ribosomal subunits and required for ribosomal large subunit biogenesis [[cite:PUB00045051], [cite:PUB00056824]].</p> <p>A number of eukaryotic and archaeabacterial ribosomal proteins can be grouped on the basis of sequence similarities. One of these families [[cite:PUB00000236]] consists of mammalian ribosomal protein eL24; yeast ribosomal protein eL24A/B; <i>Kluyveromyces lactis</i> ribosomal protein eL24; <i>Arabidopsis thaliana</i> ribosomal protein eL24y/z; <i>Haloarcula marismortui</i> ribosomal protein eL24; and <i>Methanocaldococcus jannaschii</i> protein eL24. These proteins have 60 to 160 amino-acid residues.</p> <p>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 [[cite:PUB00007068], [cite:PUB00007069]]. 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.</p> <p>Many 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 [[cite:PUB00007069], [cite:PUB00007070]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 12

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: