Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (22)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Esen, A.
Right arrow Articles by Blanchard, D. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Esen, A.
Right arrow Articles by Blanchard, D. J.
Agricola
Right arrow Articles by Esen, A.
Right arrow Articles by Blanchard, D. J.

Plant Physiol, February 2000, Vol. 122, pp. 563-572

A Specific beta -Glucosidase-Aggregating Factor Is Responsible for the beta -Glucosidase Null Phenotype in Maize1

Asim Esen* and David J. Blanchard

Department of Biology, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24060-0406.

Maize (Zea mays L.) beta -glucosidase was extracted from shoots of a wild-type (K55) and a "null" (H95) maize genotype. Enzyme activity assays and electrophoretic data showed that extracts from the null genotype had about 10% of the activity present in the normal genotype. Zymograms of the null genotype were devoid of any activity bands in the resolving gel, but had a smeared zone of activity in the stacking gel after native polyacrylamide gel electrophoresis. When extracts were made with buffers containing 0.5% to 2% sodium dodecyl sulfate, the smeared activity zone entered the resolving gel as a distinct band. These data indicated that the null genotypes have beta -glucosidase activity, but the enzyme occurs as insoluble or poorly soluble large quaternary complexes mediated by a beta -glucosidase-aggregating factor (BGAF). BGAF is a 35-kD protein and binds specifically to beta -glucosidase and renders it insoluble during extraction. BGAF also precipitates beta -glucosidase that is added exogenously to supernatant fluids of the null tissue extracts. The specific beta -glucosidase-aggregating activity of BGAF is unequivocally demonstrated. These data clearly show that the monogenic inheritance reported for the null alleles at the beta -glucosidase gene is actually for the BGAF protein, and BGAF is solely responsible for beta -glucosidase aggregation and insolubility and, thus, the apparent null phenotype.

1 This research was supported in part by a Jeffress Foundation grant.

* Corresponding author; e-mail aevatan{at}vt.edu; fax 540-231-9307.

© 2000 American Society of Plant Physiologists


This article has been cited by other articles:


Home page
 GlycobiologyHome page
F. S Kittur, H. Y. Yu, D. R Bevan, and A. Esen
Homolog of the maize {beta}-glucosidase aggregating factor from sorghum is a jacalin-related GalNAc-specific lectin but lacks protein aggregating activity
Glycobiology, March 1, 2009; 19(3): 277 - 287.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
A. J. Nagano, Y. Fukao, M. Fujiwara, M. Nishimura, and I. Hara-Nishimura
Antagonistic Jacalin-Related Lectins Regulate the Size of ER Body-Type {beta}-Glucosidase Complexes in Arabidopsis thaliana
Plant Cell Physiol., June 1, 2008; 49(6): 969 - 980.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
V. Coneva, T. Zhu, and J. Colasanti
Expression differences between normal and indeterminate1 maize suggest downstream targets of ID1, a floral transition regulator in maize
J. Exp. Bot., October 10, 2007; (2007) erm217v1.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. S. Kittur, M. Lalgondar, H. Y. Yu, D. R. Bevan, and A. Esen
Maize beta-Glucosidase-aggregating Factor Is a Polyspecific Jacalin-related Chimeric Lectin, and Its Lectin Domain Is Responsible for beta-Glucosidase Aggregation
J. Biol. Chem., March 9, 2007; 282(10): 7299 - 7311.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
M. Sue, K. Yamazaki, S. Yajima, T. Nomura, T. Matsukawa, H. Iwamura, and T. Miyamoto
Molecular and Structural Characterization of Hexameric beta-D-Glucosidases in Wheat and Rye
Plant Physiology, August 1, 2006; 141(4): 1237 - 1247.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
A. J. Nagano, R. Matsushima, and I. Hara-Nishimura
Activation of an ER-body-localized {beta}-Glucosidase via a Cytosolic Binding Partner in Damaged Tissues of Arabidopsis thaliana
Plant Cell Physiol., July 1, 2005; 46(7): 1140 - 1148.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
R. Matsushima, Y. Fukao, M. Nishimura, and I. Hara-Nishimura
NAI1 Gene Encodes a Basic-Helix-Loop-Helix-Type Putative Transcription Factor That Regulates the Formation of an Endoplasmic Reticulum-Derived Structure, the ER Body
PLANT CELL, June 1, 2004; 16(6): 1536 - 1549.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
S. Eriksson, E. Andreasson, B. Ekbom, G. Graner, B. Pontoppidan, J. Taipalensuu, J. Zhang, L. Rask, and J. Meijer
Complex Formation of Myrosinase Isoenzymes in Oilseed Rape Seeds Are Dependent on the Presence of Myrosinase-Binding Proteins
Plant Physiology, August 1, 2002; 129(4): 1592 - 1599.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. J. Blanchard, M. Cicek, J. Chen, and A. Esen
Identification of beta -Glucosidase Aggregating Factor (BGAF) and Mapping of BGAF Binding Regions on Maize beta -Glucosidase
J. Biol. Chem., April 6, 2001; 276(15): 11895 - 11901.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2000 by the American Society of Plant Biologists