Structural Requirements for Bacterial Expression of Stable, Enzymatically Active Fusion Proteins Containing the Human Immunodeficiency Virus Reverse Transcriptase

Naoko Tanese, Vinayaka R. Prasad, Stephen P. Goff

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

A collection of variant plasmids that express the human immunodeficiency virus (HIV) reverse transcriptase as trpE fusion proteins were generated and scored for their ability to produce stable, active proteins. Trimming portions of the viral pol gene resulted in dramatic increases in yield over earlier constructs; the accumulation of high levels of enzymatically active protein in this system was increased by the retention of the trpE sequences at the amino terminus. A new in situ gel activity assay was used to demonstrate that the major induced protein, containing approximately 68 kD of viral sequences, was the active species.

Original languageEnglish (US)
Pages (from-to)407-416
Number of pages10
JournalDNA
Volume7
Issue number6
DOIs
Publication statusPublished - Jul 1988
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics

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