Diamond-Blackfan anemia (DBA) is a congenital erythroid aplasia characterized as 
a normochromic macrocytic anemia with a selective deficiency in red blood cell 
precursors in otherwise normocellular bone marrow. In 40% of DBA patients, 
various physical anomalies are also present. Currently two genes are associated 
with the DBA phenotype--the ribosomal protein (RP) S19 mutated in 25% of DBA 
patients and RPS24 mutated in approximately 1.4% of DBA patients. Here we report 
the identification of a mutation in yet another ribosomal protein, RPS17. The 
mutation affects the translation initiation start codon, changing T to G 
(c.2T>G), thus eliminating the natural start of RPS17 protein biosynthesis. RNA 
analysis revealed that the mutated allele was expressed, and the next downstream 
start codon located at position +158 should give rise to a short peptide of only 
four amino acids (Met-Ser-Arg-Ile). The mutation arose de novo, since all 
healthy family members carry the wild-type alleles. The identification of a 
mutation in the third RP of the small ribosomal subunit in DBA patients further 
supports the theory that impaired translation may be the main cause of DBA 
pathogenesis.