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Expression, purification, and DNA-binding activity of the Herbaspirillum seropedicae RecX protein
- Source :
-
Protein Expression & Purification . Jun2004, Vol. 35 Issue 2, p298-303. 6p. - Publication Year :
- 2004
-
Abstract
- The Herbaspirillum seropedicae RecX protein participates in the SOS response: a process in which the RecA protein plays a central role. The RecX protein of the H. seropedicae, fused to a His-tag sequence (RecX His-tagged), was over-expressed in Escherichia coli and purified by metal-affinity chromatography to yield a highly purified and active protein. DNA band-shift assays showed that the RecX His-tagged protein bound to both circular and linear double-stranded DNA and also to circular single-stranded DNA. The apparent affinity of RecX for DNA decreased in the presence of Mg2+ ions. The ability of RecX to bind DNA may be relevant to its function in the SOS response. [Copyright &y& Elsevier]
- Subjects :
- *DNA
*GENES
*NUCLEIC acids
*ESCHERICHIA coli
Subjects
Details
- Language :
- English
- ISSN :
- 10465928
- Volume :
- 35
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Protein Expression & Purification
- Publication Type :
- Academic Journal
- Accession number :
- 13061082
- Full Text :
- https://doi.org/10.1016/j.pep.2004.01.014