Overproduction, purification and crystallization of TaqI restriction endonuclease. Academic Article uri icon

Overview

abstract

  • Under phoA promoter control, TaqI endonuclease was overproduced to 5% of Escherichia coli cellular proteins. This was achieved by fusing the endonuclease gene to the first four codons of the alkaline phosphatase signal sequence. For maximal overproduction (30% of cellular proteins), a putative 14-bp hairpin within the endonuclease coding sequence was replaced with degenerate codons. In addition, TaqI methylase was required to protect host DNA. The endonuclease was purified in sufficient amounts for crystallization.

publication date

  • May 30, 1988

Research

keywords

  • DNA Restriction Enzymes
  • Deoxyribonucleases, Type II Site-Specific
  • Gene Expression Regulation

Identity

Scopus Document Identifier

  • 0023904810

Digital Object Identifier (DOI)

  • 10.1016/0378-1119(88)90453-2

PubMed ID

  • 2842231

Additional Document Info

volume

  • 65

issue

  • 2