Abstract:
:Tripeptidyl-peptidase II (TPP II) is a cytosolic peptidase that has been implicated in fat formation and cancer, apparently independent of the enzymatic activity. In search for alternative functional regions, conserved motifs were identified and eleven signatures were constructed. Seven of the signatures covered previously investigated residues, whereas the functional importance of the other motifs is unknown. This provides directions for future investigations of alternative activities of TPP II. The obtained signatures provide an efficient bioinformatic tool for the identification of TPP II homologues. Hence, a TPP II sequence homologue from fission yeast, Schizosaccharomyces pombe, was identified and demonstrated to encode the TPP II-like protein previously reported as multicorn. Furthermore, an homologous protein was found in the prokaryote Blastopirellula marina, albeit the TPP II function was apparently not conserved. This gene is probably the result of a rare gene transfer from eukaryote to prokaryote.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Eriksson S,Gutiérrez OA,Bjerling P,Tomkinson Bdoi
10.1016/j.abb.2009.01.007subject
Has Abstractpub_date
2009-04-01 00:00:00pages
39-45issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(09)00005-8journal_volume
484pub_type
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