InterPro : IPR002136

Name  Ribosomal protein L4/L1e Short Name  Ribosomal_L4/L1e
Type  Family Description  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 [, ]. 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 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 [, ].This family includes ribosomal L4/L1 from eukaryotes and plants and L4 from bacteria. L4 from yeast has been shown to bind rRNA []. These proteins have 246 (plant) to 427 (human) amino acids.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

2 Child Features

Id Name Short Name Type
IPR013005 Ribosomal protein L4/L1e, bacterial-type Ribosomal_L4/L1e_bac-type Family
IPR019970 Ribosomal protein L4 Ribosomall_L4 Family

1 Contains

Id Name Short Name Type
IPR013000 Ribosomal protein L4/L1e, eukaryotic/archaeal, conserved site Ribosomal_L4/L1e_euk/arc_CS Conserved_site

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Ramakrishnan V Atomic structures at last: the ribosome in 2000. 2001 Curr Opin Struct Biol 11 144-54
Maguire BA The ribosome in focus. 2001 Cell 104 813-6
Chandra Sanyal S The end of the beginning: structural studies of ribosomal proteins. 2000 Curr Opin Struct Biol 10 633-6
Yeh LC Yeast ribosomal proteins L4, L17, L20, and L25 exhibit different binding characteristics for the yeast 35S precursor rRNA. 1998 Biochim Biophys Acta 1443 139-48



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)