Disease relevance of rpmJ

• The metal binding properties of the CCCH motif of the 50S ribosomal protein L36 from Thermus thermophilus [1].
• From these results we conclude that the secX gene in E. coli and in plant chloroplasts encodes a small (37-38 amino acid residues) ribosomal protein belonging to the 50S subunit [2].

High impact information on rpmJ

• We now show that the open reading frame X indeed directs the synthesis of a protein with electrophoretic mobilities similar to the B protein, and this supports the proposal that X may be more appropriately called rpmJ [3].
• We conclude that proteins A and B are intrinsic ribosomal proteins, and propose calling their genes, rpmI and rpmJ, respectively [4].
• Nucleotide sequence and linkage map position of the secX gene in maize chloroplast and evidence that it encodes a protein belonging to the 50S ribosomal subunit [2].
• The derived amino acid sequence of maize chloroplast secX is 95%, 87% and 62% identical to the corresponding derived amino acid sequences from two plant chloroplasts and Escherichia coli, respectively [2].

Analytical, diagnostic and therapeutic context of rpmJ

• Spinach chloroplast 50S subunit proteins separated by HPLC also gave a peak corresponding to pure secX protein [2].

References