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M008872200v1
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Papers In Press, published online ahead of print November 28, 2000
J. Biol. Chem, 10.1074/jbc.M008872200
Submitted on September 28, 2000
Revised on November 28, 2000
Accepted on November 27, 2000

Identification of Beta-glucosidase Aggregating Factor (BGAF) and Mapping of BGAF binding Regions on Maize Beta-Glucosidase

David J. Blanchard, Muzaffer Cicek, Jialun Chen, and Asim Esen

Biology, Virginia Polytechnic Institute & State University, Blacksburg, VA 24061-0406

Corresponding Author: aevatan{at}vt.edu

In certain maize genotypes (nulls), b-glucosidase does not enter the gel and therefore cannot be detected on zymograms. Such genotypes were initially thought to be homozygous for a null allele at the glu1 gene. We have shown that a b-glucosidase aggregating factor (BGAF) is responsible for the null phenotype, and it specifically interacts with maize ß-glucosidases and forms large insoluble aggregates. To understand the mechanism of the ß-glucosidase-BGAF interaction, we constructed chimeric enzymes by domain swapping between the maize ß-glucosidase isozymes Glu1 and Gu2, to which BGAF binds, and the sorghum ß-glucosidase (dhurrinase) isozyme Dhr1, to which BGAF does not bind. The results of binding assays with 12 different chimeric enzymes showed that an N-terminal region (E50-V145) and an extreme C-terminal region (F466-A512) together form the BGAF binding site on the enzyme surface. In addition, we purified BGAF, determined its N-terminal sequence, amplified the BGAF cDNA by RT-PCR, expressed it in E. coli and showed that it encodes a protein whose binding and immunological properties are identical to the native BGAF isolated from maize tissues. A database search revealed that BGAF is a member of the small heat shock protein family. Interestingly, the deduced BGAF sequence contained an octapeptide sequence (GP/RWGGSGG) repeated twice. Each of these repeat units is postulated to be involved in forming a site for binding to maize ß-glucosidases, and thus providing a plausible explanation for the divalent function of BGAF predicted from binding assays.


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