NDLI: P22 Arc repressor: enhanced expression of unstable mutants by addition of polar C-terminal sequences.

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P22 Arc repressor: enhanced expression of unstable mutants by addition of polar C-terminal sequences.

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P22 Arc repressor: enhanced expression of unstable mutants by addition of polar C-terminal sequences.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Brown, B. M. Milla, M. E. Sauer, R. T.
Description	Author Affiliation: Milla ME ( Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.)
Abstract	Many mutant variants of the P22 Arc repressor are subject to intracellular proteolysis in Escherichia coli, which precludes their expression at levels sufficient for purification and subsequent biochemical characterization. Here we examine the effects of several different C-terminal extension sequences on the expression and activity of a set of Arc mutants. We show that two tail sequences, KNQHE (st5) and H6KNQHE (st11), increase the expression levels of most mutants from 10- to 20-fold and, in some cases, result in restoration of biological activity in the cell. A third tail sequence, HHHHHH (st6), was not as effective in increasing mutant expression levels. All three tail sequences are functionally and structurally silent, as judged by their lack of effects on the DNA binding activity and stability of otherwise wild-type Arc. The properties of the st11 tail sequence make it an efficient system for the expression and purification of mutant Arc proteins, both because mutant expression levels are increased and because the proteins can be rapidly purified using nickel-chelate affinity chromatography. Arc mutants containing the EA28, RL31, and SA32 mutations were purified in the st11 background. The thermodynamic stability of the EA28 mutant (delta delta Gu approximately -0.4 kcal/mol) is reduced modestly compared to the st11 parent, whereas the RL31 mutant (delta delta Gu approximately -3.0 kcal/mol) and SA32 mutant (delta delta Gu approximately -3.3 kcal/mol) are substantially less stable.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	12
Volume Number	2
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1993-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Dna-binding Proteins Biosynthesis Escherichia Coli Metabolism Repressor Proteins Viral Proteins Amino Acid Sequence Cell Division Genetics Growth & Development Models, Chemical Molecular Sequence Data Mutation Oligopeptides Protein Denaturation Recombinant Proteins Drug Effects Sequence Homology, Amino Acid Suppression, Genetic Urea Pharmacology Viral Regulatory And Accessory Proteins Comparative Study Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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