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- Title
Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity
- Authors
Jiménez, Alberto; Johansson, Catrine; Ljung, Johanna; Sagemark, Johan; Berndt, Kurt D.; Ren, Bin; Tibbelin, Gudrun; Ladenstein, Rudolf; Kieselbach, Thomas; Holmgren, Arne; Gustafsson, Jan-Åke; Miranda-Vizuete, Antonio
- Abstract
Spermatid-specific thioredoxin-1 (Sptrx-1) is the first member of the thioredoxin family of proteins with a tissue-specific expression pattern, found exclusively in the tail of elongating spermatids and spermatozoa. We describe here further biochemical characterization of human Sptrx-1 protein structure and enzymatic activity. In gel filtration chromatography human Sptrx-1 eluates as a 400 kDa protein consistent with either an oligomeric form, not maintained by intermolecular disulfide bonding, and/or a highly asymmetrical structure. Analysis of circular dichroism spectra of fragments 1–360 and 361–469 and comparison to spectra of full-length Sptrx-1 supports a two-domain organization with a largely unstructured N-terminal domain and a folded thioredoxin-like C-terminal domain. Functionally, Sptrx-1 behaves as an oxidant in vitro when using selenite, but not oxidized glutathione, as electron acceptor. This oxidizing enzymatic activity suggests that Sptrx-1 might govern the stabilization (by disulfide cross-linking) of the different structures in the developing tail of spermatids and spermatozoa.
- Subjects
THIOREDOXIN; PROTEINS
- Publication
FEBS Letters, 2002, Vol 530, Issue 1-3, p79
- ISSN
0014-5793
- Publication type
Article