Tesis doctoral de Briceño Domínguez Verónica María
One of the most remarkable features of the large ribosomal subunit is the presence of a highly flexible protuberance called the stalk. This protein complex is universally conserved and plays a central role in the ribosome-mediated translation factor activity. However, the organization and functions of the proteins constituting the stalk remain unclear. In bacteria the stalk is made of one copy of protein l10 and two dimers of the acidic protein l7/l12; while in eukaryotes it is composed by p0 (l10 protein-equivalent) and two heterodimers of the acidic proteins p1 and p2. In saccharomyces cerevisiae, two additional subgroups are distinguished, p1 /p1 and p2 /p2 which form biologically relevant heterodimers, p1 -p2 and p1 -p2 . The fact that in eukaryotes have two different ribosomal families, while in prokaryotes ones have only one, suggest a specialization of functions between both groups. Some data indicate that p1 and p2 proteins have different roles in the assembly and functions of the stalk. However, nowadays the information is very scarce about the possible roles of the two protein types in the stalk function, and some structural features are still unclear. the experiments presented here were designed to explore the different roles that the p1 and p2 proteins may have in the stalk activity, and to characterize more precisely the regions involved in their binding to ribosomes and between them. To fulfil these aims, we designed two series of protein chimeras, comprising consecutively larger and complementary fragments of proteins p1 and p2 , which contained well defined secondary structure elements. These proteins were expressed in yeast strains lacking the corresponding native proteins and the presence of the chimeras in the ribosomes was tested. Similarly, the proteins chimeras were tested using the two-hybrids system to analyze the interactions with the corresponding native proteins. The results allowed us to conclude that the amino acid sequence of th
Datos académicos de la tesis doctoral «Análisis de las regiones de las proteínas p1a y p2b que determinan su especificidad estructural y funcional en el tallo ribosómico de saccharomyces cerevisiae«
- Título de la tesis: Análisis de las regiones de las proteínas p1a y p2b que determinan su especificidad estructural y funcional en el tallo ribosómico de saccharomyces cerevisiae
- Autor: Briceño Domínguez Verónica María
- Universidad: Autónoma de Madrid
- Fecha de lectura de la tesis: 15/06/2007
Dirección y tribunal
- Director de la tesis
- Juan Pedro García Ballesta
- Tribunal
- Presidente del tribunal: Luis Revuelta josé
- De la cruz Jesús (vocal)
- encarna Martínez (vocal)
- ángel Rodríguez Miguel (vocal)