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Literature summary for 3.2.1.31 extracted from

  • Worley, C.K.; Ling, R.; Callis, J.
    Engineering in vivo instability of firefly luciferase and Escherichia coli beta-glucuronidase in higher plants using recognition elements from the ubiquitin pathway (1998), Plant Mol. Biol., 37, 337-347.
    View publication on PubMed

Application

Application Comment Organism
analysis reporter enzyme which is used for studies in higher plants because endogenous activities are low and sensitive assays are available. A version of GUS with phenylalanine at the mature N-terminus accumulates a minimum of 3fold lower than GUS with methionine at its mature N-terminus. This altered protein can be useful for promoter studies which require more rapid changes in the accumulation of the reporter protein Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information the enzyme is engineered as fusion with an N-terminal 76 amino acid ubiquitin-coding region. When translated in any eukaryotic cell, such ubiquitin fusions are cleaved by ubiqitin-specific proteases specifically after the C-terminus of ubiquitin, irrespective of the distal amino acid (with the exception of Pro), releasing the downstream protein with the specified amino terminus. The presence of an N-terminal uncleavable ubiquitin on GUS does not reduce activity. A version of GUS with phenylalanine at the mature N-terminus accumulates a minimum of 3fold lower than GUS with methionine at its mature N-terminus Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Synonyms

Synonyms Comment Organism
beta-glucuronidase
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Escherichia coli
GUS
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Escherichia coli