Identification and characterization of a ubiquitinconjugating enzyme UBE2A gene from lamprey.

Abstract

Ubiquitin-conjugating enzymes (E2s) play an important role in the mechanism of ubiquitin transfer. Although in most species many of these enzymes share high sequence and structural conservation, their existence and functions in the lamprey remain unknown. In this study, we identified and characterized a ubiquitin-conjugating enzyme (UBE2A)-like gene in lamprey. The gene, designated as LaUBE2A, contained a 456-bp open reading frame encoding a 152-amino acid protein with a typical UBC domain. Real-time PCR assay showed that LaUBE2A was expressed in various tissues of the adult lamprey, with higher levels in the leukocytes and muscle and lower levels in the skin and liver. The high conservation in amino acid sequence between LaUBE2A and UBE2As from Homo sapiens, Mus musculus, Cavia porcellus, and Alligator sinensi implied that the function of LaUBE2A may be similar to that of UBE2A.