Ubiquitin of Entamoeba histolytica deviates in six amino acid residues from the consensus of all other known ubiquitins

FEBS Letters

Tannich, Egbert¹  Bakker-Grunwald, Tilly²  Wöstmann, Claudia² 

[1] Bernhard-Nocht-Institut, D-2000 Hamburg, Germany;Universität Osnabrück, Abteilung Mikrobiologie, Barbarastrasse 11, D-4500 Osnabrück, Germany

关键词: Eukaryote evolution;    Ubiquitin;    Entamoeba;    SDS-PAGE;    sedium dodecyl sulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(92)81049-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The amino acid sequence of ubiquitin from Entamoeba histolytica, as deduced from a cDNA nucleotide sequence, deviated a six positions from the consensus of all other known ubiquitins (ranging from Trypanosoma cruzi to Homo sapiens). The corresponding residues were scattered over the primary sequence, but came close together on the surface of the folded protein structure. We conclude that (i) E. histolytica branched off very early from the main eukaryotic line, and (ii) this organism may yield clues as to the evolutionary development of the ubiquitin system.

【 授权许可】

Unknown