High impact information on RpL40

• The present results show that the 5' regulatory region of DUb52 shares common features with the ribosomal protein genes of Drosophila, Xenopus and mouse, including GC- and pyrimidine-rich regions [1].
• We report here the organization and expression of a third member, the DUb52 gene, isolated by screening a Drosophila melanogaster genomic library [1].
• As in other eukaryotes, the N-terminal region of the deduced amino-acid sequence is a ubiquitin moiety and the C-terminal region CEP52, a protein component of the large ribosomal subunit [2].
• Northern analysis indicates that A. millepora Ub52 is encoded by a small (< 800 nt) mRNA present in eggs and is first expressed after the early gastrula stage in embryonic development [2].
• Stained two-dimensional gels indicate that the quantity of CEP52 associated with ribosomes is similar to that of other ribosomal proteins of corresponding size [3].

Analytical, diagnostic and therapeutic context of RpL40

• The size of the immunoreactive polypeptide indicates that CEP52 is cleaved from ubiquitin and this apparent proteolytic processing was confirmed by amino-terminal sequence analysis of CEP52 isolated by two-dimensional gel electrophoresis [3].

References