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- Title
Efficient expression of truncated recombinant cadmium-metallothionein gene of a ciliate, <i>Tetrahymena tropicalis lahorensis</i> in <i>Escherichia coli</i>.
- Authors
Shuja, Rukhsana Nighat; Taimuri, Shuja Uddin Ahmad; Shakoori, Farah Rauf; Shakoori, Abdul Rauf
- Abstract
Truncated recombinant metallothionein GST–fusion protein has been successfully expressed in Escherichia coli. The previously identified novel Cd-inducible metallothionein ( TMCd1) gene from the locally isolated ciliate, Tetrahymena tropicalis lahorensis, was inserted into a pET-41a vector, in frame with a sequence encoding an N-terminal glutathione- S-transferase (GST) tail. Truncated recombinant GST fusion protein has been purified by affinity column chromatography using glutathione sepharose. After enzymatic cleavage of GST tail with enterokinase, the truncated TMCd1 MT shows molecular weight of 11.5 kDa, corresponding to the expected value. This is the first successful report of expression of cadmium metallothionein gene of a ciliate, T. t. lahorensis, reported from this part of the world, in E. coli. This study will further help in characterization of metallothionein protein of this ciliate.
- Subjects
GENE expression; METALLOTHIONEIN genetics; CHIMERIC proteins; GLUTATHIONE transferase; CILIATA; ESCHERICHIA coli
- Publication
Molecular Biology Reports, 2013, Vol 40, Issue 12, p7061
- ISSN
0301-4851
- Publication type
Article
- DOI
10.1007/s11033-013-2827-5