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Heterologously expressed polypeptide from the yeast meiotic gene HOP1 binds preferentially to yeast DNA.

Abstract:

HOP1 protein, present in sporulating cells of Saccharomyces cerevisiae and believed to be a component of the synaptonemal complex, has been expressed in Escherichia coli fused to a biotinylated tag protein. Once solubilized from bacterial inclusion bodies, the HOP1 fusion protein was purified by using a combination of avidin-affinity chromatography and gel filtration FPLC and refolded. Sequence comparisons indicate that the HOP1 gene product contains a zinc finger motif, which may confer DNA ...

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Publication status:
Published

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Publisher copy:
10.1006/prep.1999.1052

Authors


Alché, JD More by this author
Dickinson, H More by this author
Journal:
Protein expression and purification
Volume:
16
Issue:
2
Pages:
251-260
Publication date:
1999-07-05
DOI:
EISSN:
1096-0279
ISSN:
1046-5928
URN:
uuid:343f1c68-9f60-4619-a266-b3d05de0b09d
Source identifiers:
53208
Local pid:
pubs:53208

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