| Autor: |
Leong, Vivian, Kent, Meredith, Jomaa, Ahmad, Ortega, Joaquin |
| Zdroj: |
RNA; June 2013, Vol. 19 Issue: 6 p789-802, 14p |
| Abstrakt: |
We still do not have a complete understanding of all the steps in the assembly and maturation of the ribosome despite recent progress in this area. In this study, Leong et al. used cryo-EM and mass spectrometry to examine the immature 30S particles that accumulate in strains lacking the late-stage assembly factor RimM. Their studies show that the particles isolated from ΔrimMmutants, like those of ΔyjeQmutants (RNA17:697), lack densities corresponding to helices 44 and 45. In addition, tertiary ribosomal proteins are depleted in the particles. These observations support a model in which multiple parallel assembly pathways converge into a late assembly intermediate; functionally related proteins then act simultaneously or sequentially to catalyze the final steps of 30S maturation. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
