2V94

Crystal structure of P. abyssi RPS24

Summary for 2V94

• Entry DOI: 10.2210/pdb2v94/pdb
• Descriptor: 30S RIBOSOMAL PROTEIN S24E (2 entities in total)
• Functional Keywords: ribosomal protein, ribonucleoprotein
• Biological source: PYROCOCCUS ABYSSI
• Total number of polymer chains: 2
• Total formula weight: 26052.81

Authors

Legrand, P.,Pinaud, N.,Gleizes, P.E.,Fribourg, S. (deposition date: 2007-08-21, release date: 2008-04-29, Last modification date: 2024-11-06)

Primary citation

Choesmel, V.,Fribourg, S.,Aguissa-Toure, A.H.,Pinaud, N.,Legrand, P.,Gazda, H.T.,Gleizes, P.E.
Mutation of Ribosomal Protein Rps24 in Diamond- Blackfan Anemia Results in a Ribosome Biogenesis Disorder.
Hum.Mol.Genet., 17:1253-, 2008

PubMed Abstract: Diamond-Blackfan anemia (DBA) is a rare congenital disease affecting erythroid precursor differentiation. DBA is emerging as a paradigm for a new class of pathologies potentially linked to disorders in ribosome biogenesis. Three genes encoding ribosomal proteins have been associated to DBA: after RPS19, mutations in genes RPS24 and RPS17 were recently identified in a fraction of the patients. Here, we show that cells from patients carrying mutations in RPS24 have defective pre-rRNA maturation, as in the case of RPS19 mutations. However, in contrast to RPS19 involvement in the maturation of the internal transcribed spacer 1, RPS24 is required for processing of the 5' external transcribed spacer. Remarkably, epistasis experiments with small interfering RNAs indicate that the functions of RPS19 and RPS24 in pre-rRNA processing are connected. Resolution of the crystal structure of RPS24e from the archeon Pyroccocus abyssi reveals domains of RPS24 potentially involved in interactions with pre-ribosomes. Based on these data, we discuss the impact of RPS24 mutations and speculate that RPS19 and RPS24 cooperate at a particular stage of ribosome biogenesis connected to a cell cycle checkpoint, thus affecting differentiation of erythroid precursors as well as developmental processes.

PubMed: 18230666
DOI: 10.1093/HMG/DDN015

Experimental method

X-RAY DIFFRACTION (1.9 Å)