Expression of mutant patatin protein in transgenic tobacco plants: role of glycans and intracellular location. (original) (raw)

Journal Article

,

Institut für Genbiologische Forschung Berlin GmbH, Federal Republic of Germany.

Search for other works by this author on:

,

Institut für Genbiologische Forschung Berlin GmbH, Federal Republic of Germany.

Search for other works by this author on:

Institut für Genbiologische Forschung Berlin GmbH, Federal Republic of Germany.

Search for other works by this author on:

Cite

U Sonnewald, A von Schaewen, L Willmitzer, Expression of mutant patatin protein in transgenic tobacco plants: role of glycans and intracellular location., The Plant Cell, Volume 2, Issue 4, April 1990, Pages 345–355, https://doi.org/10.1105/tpc.2.4.345
Close

Navbar Search Filter Mobile Enter search term Search

Abstract

The influence of N-glycosylation and subcellular compartmentation on various characteristics of a vacuolar glycoprotein is described. One member of the patatin gene family was investigated as a model system. Different glycosylation mutants obtained by destroying the consensus site Asn-X-Ser/Thr by oligonucleotide-directed mutagenesis were expressed in leaves of transgenic tobacco plants under the control of a light-inducible promoter. The various patatin glycomutants retained their properties in comparison with the wild-type protein with respect to protein stability, subcellular compartmentation, enzymatic activity, and various physicochemical properties studied showing the N-glycosylation not to be essential for any of these characteristics. To test the importance of the cotranslational transport and the subcellular (vacuolar) location for the properties of the patatin protein, another mutant was constructed in which the signal peptide was deleted, leading to its synthesis and accumulation in the cytosol. Biochemical analysis of this protein in comparison with its vacuolar form again revealed no significant differences with respect to its enzymatic activity or its stability in normal vegetative cells. During seed development, however, the cytoplasmic form was more stable than the vacuolar form, indicating the appearance of proteases specific for the protein bodies of developing seeds.

This content is only available as a PDF.

© 1990 by American Society of Plant Biologists

This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open\_access/funder\_policies/chorus/standard\_publication\_model)

Citations

Views

Altmetric

Metrics

Total Views 66

0 Pageviews

66 PDF Downloads

Since 8/1/2021

Month: Total Views:
August 2021 6
September 2021 1
October 2021 3
November 2021 3
December 2021 4
January 2022 1
February 2022 4
March 2022 2
April 2022 2
May 2022 2
June 2022 6
July 2022 2
September 2022 3
October 2022 3
January 2023 1
March 2023 1
April 2023 1
May 2023 2
June 2023 1
November 2023 2
December 2023 2
January 2024 2
March 2024 1
April 2024 4
May 2024 3
July 2024 1
August 2024 1
September 2024 2

Citations

39 Web of Science

×

Email alerts

Citing articles via

More from Oxford Academic