The search for RING domain proteins : cases arabidopsis and silver birch

Ubiquitin is an important modifier in eukaryotic cells through many effects on the targeted protein. Ubiquitination is a reaction cascade, catalyzed by E1 – E2 and finally E3 enzyme which completes the ubiquitination. In this study preselected 61 RING type ubiquitin E3 proteins of Arabidopsis thaliana were classified, grouped and analysed to characterize what kind of domains and groups were included. Proteins which contain a RING domain, can either ubiquitinate substrates independently or function as part of a multi-subunit complex. RING E3s are known to act as a molecular adaptors for the E2s and the substrates. It is the E3 ligase that is responsible for selecting the target protein for ubiquitination and later for degradation in proteasome in to peptides. The same preselected 61 genes were also researched from the Betula pendula Roth genome. Web Apollo database was used to annotate genes from the recently sequenced silver birch genome. As a result 32 gene homologs that included RING domain were identified in silver birch