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rdf:type |
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lifeskim:mentions |
umls-concept:C0380966,
umls-concept:C1326471,
umls-concept:C1514562,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1960782,
umls-concept:C2003941
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pubmed:issue |
29
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pubmed:dateCreated |
2007-12-6
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pubmed:abstractText |
We have analyzed the highly conserved N-terminus of Hansenula polymorpha Pex14p for its function in peroxisomal matrix protein import. The region comprising aa 10-54 of HpPex14p is predicted to contain three alpha-helices. Its alpha-helical structure was confirmed by CD analysis of a synthetic peptide, corresponding to residues 8-58. Deletion of aa 1-21 of HpPex14p, but not of aa 1-9, completely abolished PTS1 and PTS2 matrix protein import. An extensive mutational analysis of the first alpha-helix (aa 10-21) demonstrated that its secondary structure, as well as residues Phe20 and Leu21, are essential for PTS1 and PTS2 matrix protein import.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
581
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5627-34
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pubmed:meshHeading |
pubmed-meshheading:18023285-Amino Acid Sequence,
pubmed-meshheading:18023285-Circular Dichroism,
pubmed-meshheading:18023285-Conserved Sequence,
pubmed-meshheading:18023285-Fungal Proteins,
pubmed-meshheading:18023285-Membrane Proteins,
pubmed-meshheading:18023285-Microscopy, Fluorescence,
pubmed-meshheading:18023285-Molecular Sequence Data,
pubmed-meshheading:18023285-Pichia,
pubmed-meshheading:18023285-Protein Structure, Tertiary,
pubmed-meshheading:18023285-Protein Transport,
pubmed-meshheading:18023285-Receptors, Cytoplasmic and Nuclear
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pubmed:year |
2007
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pubmed:articleTitle |
A conserved alpha helical domain at the N-terminus of Pex14p is required for PTS1 and PTS2 protein import in Hansenula polymorpha.
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pubmed:affiliation |
Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, 9750 AA, Haren, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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