Unknown

Dataset Information

0

Eukaryote-specific extensions in ribosomal proteins of the small subunit: Structure and function.


ABSTRACT: High-resolution structures of yeast ribosomes have improved our understanding of the architecture and organization of eukaryotic rRNA and proteins, as well as eukaryote-specific extensions present in some conserved ribosomal proteins. Despite this progress, assignment of specific functions to individual proteins and/or eukaryote-specific protein extensions remains challenging. It has been suggested that eukaryote-specific extensions of conserved proteins from the small ribosomal subunit may facilitate eukaryote-specific reactions in the initiation phase of protein synthesis. This review summarizes emerging data describing the structural and functional significance of eukaryote-specific extensions of conserved small ribosomal subunit proteins, particularly their possible roles in recruitment and spatial organization of eukaryote-specific initiation factors.

SUBMITTER: Ghosh A 

PROVIDER: S-EPMC4682806 | biostudies-literature | 2015 Jan-Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Eukaryote-specific extensions in ribosomal proteins of the small subunit: Structure and function.

Ghosh Arnab A   Komar Anton A AA  

Translation (Austin, Tex.) 20150101 1


High-resolution structures of yeast ribosomes have improved our understanding of the architecture and organization of eukaryotic rRNA and proteins, as well as eukaryote-specific extensions present in some conserved ribosomal proteins. Despite this progress, assignment of specific functions to individual proteins and/or eukaryote-specific protein extensions remains challenging. It has been suggested that eukaryote-specific extensions of conserved proteins from the small ribosomal subunit may faci  ...[more]

Similar Datasets

| S-EPMC5389730 | biostudies-literature
| S-EPMC1364506 | biostudies-literature
| S-EPMC5027506 | biostudies-literature
| S-EPMC2993421 | biostudies-literature
| S-EPMC149469 | biostudies-literature
| S-EPMC5737520 | biostudies-literature
| S-EPMC102429 | biostudies-literature
| S-EPMC6352543 | biostudies-literature
| S-EPMC3223260 | biostudies-literature
| S-EPMC5915897 | biostudies-literature