| Literature DB >> 10364457 |
Abstract
We report here the existence of a subfamily of eukaryotic parvulin proteins that have strong sequence homology with E. coli parvulin, but lack the WW domain found in previously described eukarytoic parvulins. We hence term members of this subfamily EPVH (eukaryotic parvulin homologue). We describe the characterisation of hEPVH (human eukaryotic parvulin homologue). Immunogold labelling transmission electron microscopy reveals that hEPVH is preferentially localised in the mitochondrial matrix. The homology of hEPVH with its prokaryotic ancestor supports the hypothesis that this protein may have a mitochondrial function. An essential role in this organelle may explain the need for a high degree of conservation of this protein between distantly related species. Copyright 1999 Academic Press.Entities:
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Year: 1999 PMID: 10364457 DOI: 10.1006/bbrc.1999.0828
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575