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Euglena gracilis contains an Ubiquitin‐S27a homologue
Author(s) -
TorresMarquez M Eugenia,
DiazMireles Edith
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.702.2
Subject(s) - euglena gracilis , ubiquitin , ribosomal protein , biology , biochemistry , ubiquitin ligase , euglena , ribosome , giardia lamblia , ribosomal rna , amino acid , microbiology and biotechnology , gene , genetics , rna , chloroplast
Ubiquitination is a widely expressed process in eukaryotic cells. For this postraductional modification to take place, the presence of ubiquitin is necessary. Unicellular organisms, such as the parasite Giardia , have been shown to contain this 8.5kDa polypeptide. However, this ubiquitin finding does not clarify whether the presence of this polypeptide is an adaptation to the host on those organisms or the origin of the posttranslational modifier is related to eukaryotic cell evolution. Thus, the search for a ubiquitin homologue in free living protists, such as Euglena gracilis ; becomes relevant as to understand the evolution of signal transduction elements. We were able to find in a E. gracilis cDNA library an Ubiquitin‐S27a protein, which consists of two main domains. The N‐terminal domain is the ubiquitin protein formed by the first 76 amino acids with a molecular weight of 8.5 kDa and a theoretical pI: 6.56. The C‐terminal ribosomal protein S27a is 81 amino acids long with a molecular weight of 9.3 kDa and a pI of 9.88. We are currently scrutinizing in our laboratory whether the ubiquitin‐like protein found in E. gracilis has a role as a protein modifier or as a chaperone at ribosomal assembly. Partly supported by Grant DGAPA219508