| Literature DB >> 16079284 |
Marleen Otzen1, Dongyuan Wang, Marcel G J Lunenborg, Ida J van der Klei.
Abstract
We have cloned and characterized the Hansenula polymorpha PEX20 gene. The HpPEX20 gene encodes a protein of 309 amino acids (HpPex20p) with a calculated molecular mass of approximately 35 kDa. In cells of an HpPEX20 disruption strain, PTS2 proteins were mislocalized to the cytosol, whereas PTS1 matrix protein import proceeded normally. Also, the PTS2 proteins amine oxidase and thiolase were normally assembled and active in these cells, suggesting HpPex20p is not involved in oligomerization/activation of these proteins. Localization studies revealed that HpPex20p is predominantly associated with peroxisomes. Using fluorescence correlation spectroscopy we determined the native molecular mass of purified HpPex20p and binding of a synthetic peptide containing a PTS2 sequence. The data revealed that purified HpPex20p forms oligomers, which specifically bind PTS2-containing peptides.Entities:
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Year: 2005 PMID: 16079284 DOI: 10.1242/jcs.02463
Source DB: PubMed Journal: J Cell Sci ISSN: 0021-9533 Impact factor: 5.285