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Title of Journal: Appl Microbiol Biotechnol

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Abbravation: Applied Microbiology and Biotechnology

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Springer-Verlag

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DOI

10.1016/0145-2134(80)90041-1

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1432-0614

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Construction of an Slayer protein exhibiting modi

Authors: Katrin Pollmann Sabine Matys
Publish Date: 2007/04/17
Volume: 75, Issue: 5, Pages: 1079-1085
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Abstract

The functional Slayer protein gene slfB of the uranium mining waste pile isolate Bacillus sphaericus JGA12 was cloned as a polymerase chain reaction product into the expression vector pET Lic/Ek 30 and heterologously expressed in Escherichia coli Bl21DE3 The addition of His tags to the N and C termini enabled the purification of the recombinant protein by Nichelating chromatography The Ni binding capacity of the Histagged recombinant Slayer protein was compared with that of the wildtype S layer The inductively coupled plasma mass spectrometry analyses demonstrate a significantly enhanced Ni binding capability of the recombinant protein In addition the selfassembling properties of the purified modified Slayer proteins were studied by light microscopy and scanning electron microscopy Whereas the wildtype Slayer proteins reassembled into regular cylindric structures the recombinant Slayer proteins reassembled into regular sheets that formed globular agglomerating structures The nanoporous structure of the protein meshwork together with its enhanced Ni binding capacity makes the recombinant Slayer attractive as a novel selfassembling biological template for the fabrication of metal nanoclusters and construction of nanomaterials that are of technical interest

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