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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Jiménez A,Johansson C,Ljung J,Sagemark J,Berndt KD,Ren B,Tibbelin G,Ladenstein R,Kieselbach T,Holmgren A,Gustafsson JA,Miranda-Vizuete Adoi
10.1016/s0014-5793(02)03417-8keywords:
subject
Has Abstractpub_date
2002-10-23 00:00:00pages
79-84issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302034178journal_volume
530pub_type
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