Manipulation of β-glucuronidase for use as a reporter in vacuolar targeting studies View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-12

AUTHORS

Leigh B. Farrell, Roger N. Beachy

ABSTRACT

It has been documented that when furnished with an endomembrane signal sequence for the endoplasmic reticulum, beta-glucuronidase (GUS) is N-glycosylated, resulting in the nearly complete loss of enzymatic activity. To enable use of beta-glucuronidase as a reporter protein in secretory and vacuolar targeting studies, one of the two putative N-linked glycosylation sites within the GUS gene was altered by site-directed mutagenesis. The second N-linked glycosylation site was not altered because sequence analysis of nucleotide sequences around the second putative glycosylation site revealed that the published sequence was incorrect, and that no such site existed. More... »

PAGES

821-825

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00039422

DOI

http://dx.doi.org/10.1007/bf00039422

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020802643

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2103475


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