Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.gene.2004.09.022
Title: The 350-fold compacted Fugu parkin gene is structurally and functionally similar to human Parkin
Authors: Yu, W.-P.
Tan, J.M.M.
Chew, K.C.M.
Oh, T.
Kolatkar, P.
Venkatesh, B.
Dawson, T.M.
Lim, K.L. 
Keywords: Dystrophin
Parkinson's disease
Transcriptional regulation
Ubiquitin ligase
Issue Date: 14-Feb-2005
Citation: Yu, W.-P., Tan, J.M.M., Chew, K.C.M., Oh, T., Kolatkar, P., Venkatesh, B., Dawson, T.M., Lim, K.L. (2005-02-14). The 350-fold compacted Fugu parkin gene is structurally and functionally similar to human Parkin. Gene 346 : 97-104. ScholarBank@NUS Repository. https://doi.org/10.1016/j.gene.2004.09.022
Abstract: Mutations in the human parkin gene (huParkin) are the predominant genetic cause of familial parkinsonism. The huParkin locus, spanning about 1.4 Mb, is one of the largest in the human genome. Despite its huge size, huParkin codes for a rather short transcript of about 4.5 kb. To gain an insight into the structure, function and evolutionary history of huParkin, we have characterized the pufferfish [Fugu rubripes (Fugu)] ortholog of huParkin. A remarkable feature of the Fugu parkin gene (fuparkin) is its unusually compact size. It spans only about 4 kb and is thus 350-fold smaller than its human ortholog. The Fugu and human parkin genes are otherwise highly similar in their genomic organization and expression pattern. Furthermore, like human Parkin, Fugu parkin also functions as an ubiquitin ligase. These shared features between fuparkin and huParkin suggest that the physiological function and regulation of the parkin gene are conserved during the evolution of vertebrates. Conceivably, the compact locus of fuparkin could serve as a useful model to understand the transcriptional regulation of huParkin. © 2004 Elsevier B.V. All rights reserved.
Source Title: Gene
URI: http://scholarbank.nus.edu.sg/handle/10635/101849
ISSN: 03781119
DOI: 10.1016/j.gene.2004.09.022
Appears in Collections:Staff Publications

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