Anti-Human RPL22 (center) Polyclonal antibody

The ubiquitous eukaryotic protein kinase CKII (casein kinase II) has been found to interact with a number of cellular proteins, either through the catalytic subunit or the regulatory subunit. Using the yeast two-hybrid screening method, we found that the catalytic subunit of Drosophila melanogaster CKII (DmCKII) interacts with Drosophila ribosomal protein L22 (rpL22). This interaction was also observed in vitro with a glutathione-S-transferase (GST)-rpL22 fusion protein. The predicted full-length Drosophila rpL22 protein has an N-terminal extension rich in alanine, lysine, and proline that appears to be unique to Drosophila. Deletion mapping revealed that the conserved core of rpL22 is responsible for the interaction with CKII. Moreover, purified DmCKII can phosphorylate a GST-L22 fusion protein at the C-terminal end, suggesting that this protein may be a substrate of CKII in Drosophila. (C) 2002 Elsevier Science (USA). All rights reserved.

Caragana intermedia is an important shrub plant with high ecological and economic value. Here, we reported and analyzed the complete chloroplast (cp) genome of C. intermedia. This cp genome is relatively short (129,331 bp) because it lacks an Inverted Repeat (IR) region. It comprises 111 genes, including four unique rRNAs, 31 tRNAs, and 76 protein-coding genes. Similar to other closely related plastomes, rpl22 and rps16 are absent, and the GC content is relatively low (31.6 %). The phylogenetic analysis suggested that C. intermedia is closely related to the genera of Astragalus.