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Título

Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity

AutorJiménez, 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
Palabras claveThioredoxin
Spermatozoon
Fibrous sheath
Redox regulation
Fecha de publicación26-sep-2002
EditorElsevier
CitaciónFEBS Letters 530(1-3): 79-84 (2002)
ResumenSpermatid-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.
Descripción24 páginas, 5 figuras.
Versión del editorhttp://dx.doi.org/10.1016/S0014-5793(02)03417-8
URIhttp://hdl.handle.net/10261/47334
DOI10.1016/S0014-5793(02)03417-8
ISSN0014-5793
E-ISSN1873-3468
ReferenciasPMID: 12387870
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