High-temperature cultivation and 5' mRNA optimization are key factors for the efficient overexpression of thermostable Deinococcus geothermalis purine nucleoside phosphorylase in Escherichia coli

Journal of Biotechnology

Volumn 156, Issue 4, 2011, Pages 268-274

  Szeker, Kathleen ^a   Niemitalo, Olli ^b   Casteleijn, Marco G ^c   Juffer, André H ^b   Neubauer, Peter ^a  

^a TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

^b UNIVERSITY OF OULU   (Finland)

^c UNIVERSITY OF HELSINKI   (Finland)

Author keywords

Deinococcus geothermalis; MRNA secondary structure; Purine nucleoside phosphorylase; Recombinant protein expression; Thermostable protein

Indexed keywords

BIOMOLECULES; ESCHERICHIA COLI; GENE EXPRESSION; PHOSPHORYLATION;

DEINOCOCCUS GEOTHERMALIS; EFFECTIVE APPROACHES; HETEROLOGOUS PROTEINS; LARGE SCALE PRODUCTIONS; PURINE NUCLEOSIDE PHOSPHORYLASE; RECOMBINANT PROTEIN EXPRESSION; SECONDARY STRUCTURES; SEQUENCE OPTIMIZATION;

RECOMBINANT PROTEINS;

5' MESSENGER RNA; MESSENGER RNA; PURINE NUCLEOSIDE PHOSPHORYLASE; UNCLASSIFIED DRUG;

ARTICLE; CELL ACTIVITY; CULTURE OPTIMIZATION; DEINOCOCCUS; DEINOCOCCUS GEOTHERMALIS; ESCHERICHIA COLI; GENE SEQUENCE; HIGH TEMPERATURE PROCEDURES; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; RNA STRUCTURE; THERMOSTABILITY; TRANSLATION INITIATION;

DEINOCOCCUS GEOTHERMALIS; ESCHERICHIA COLI;

EID: 82955247590     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.08.009     Document Type: Article

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