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Development, evaluation and application of tripeptidyl-peptidase II sequence signatures
Department of Biochemistry and Organic Chemistry, Uppsala University. (Hellgren Kotaleski Lab)
2009 (English)In: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 484, no 1, 39-45 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2009. Vol. 484, no 1, 39-45 p.
Keyword [en]
Serine protease, Subtilase, Sequence motif, Cytosolic protein degradation, Tripeptidyl-peptidase II
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:kth:diva-53381DOI: 10.1016/j.abb.2009.01.007ISI: 000264927700006PubMedID: 19467630OAI: oai:DiVA.org:kth-53381DiVA: diva2:470023
Note
QC 20111228Available from: 2011-12-28 Created: 2011-12-28 Last updated: 2017-12-08Bibliographically approved

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