Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy

doi:10.1083/jcb.79.1.10

This Article

	PDF (Full Text)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Baumgartner, B.
	Articles by Chrispeels, M. J.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Baumgartner, B.
	Articles by Chrispeels, M. J.


Social Bookmarking

	What's this?

ARTICLES

Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy

B Baumgartner, KT Tokuyasu and MJ Chrispeels

Vicilin peptidohydrolase, the protease that hydrolyzes the reserve proteins in the cotyledons of mung bean (Vigna radiata) seedlings, has been localized intracellularly by immunofluorescence microscopy using monospecific antibodies against the enzyme and rhodamine-coupled goat- anti-rabbit immunoglobulin G's. The enzyme can first be visualized after 3 days of seedling growth and is associated with small foci within the cytoplasm of the storage parenchyma cells farthest from the vascular bundles. On the 4th day of growth, the protease is also present in the numerous large protein bodies within these cells. Vicilin peptidohydrolase is known to be synthesized de novo starting on the 3rd day of growth. Our observations are therefore consistent with the interpretation that the enzyme is synthesized in the cytoplasm and subsequently transported to the protein bodies.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

Schmid, M., Simpson, D. J., Sarioglu, H., Lottspeich, F., Gietl, C. (2001). The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 10.1073/pnas.061038298v1 [Abstract] [Full Text]
Chrispeels, M. J., Herman, E. M. (2000). Endoplasmic Reticulum-Derived Compartments Function in Storage and as Mediators of Vacuolar Remodeling via a New Type of Organelle, Precursor Protease Vesicles. Plant Physiol. 123: 1227-1234 [Full Text]
Toyooka, K., Okamoto, T., Minamikawa, T. (2000). Mass Transport of Proform of a KDEL-tailed Cysteine Proteinase (SH-EP) to Protein Storage Vacuoles by Endoplasmic Reticulum-derived Vesicle Is Involved in Protein Mobilization in Germinating Seeds. JCB 148: 453-464 [Abstract] [Full Text]
Okomoto, T., Minamikawa, T., Edward, G., Vakharia, V., Herman, E. (1999). Posttranslational Removal of the Carboxyl-terminal KDEL of the Cysteine Protease SH-EP Occurs Prior to Maturation of the Enzyme. J. Biol. Chem. 274: 11390-11398 [Abstract] [Full Text]
Herman, E. M., Larkins, B. A. (1999). Protein Storage Bodies and Vacuoles. Plant Cell 11: 601-614 [Full Text]
Schmid, M., Simpson, D. J., Sarioglu, H., Lottspeich, F., Gietl, C. (2001). The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 98: 5353-5358 [Abstract] [Full Text]