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J. Biol. Chem., Vol. 276, Issue 15, 11895-11901, April 13, 2001
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From the Department of Biology, Virginia Polytechnic Institute and
State University, Blacksburg, Virginia 24061-0406
In certain maize genotypes (nulls),
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF232008.
Identification of
-Glucosidase Aggregating Factor (BGAF) and
Mapping of BGAF Binding Regions on Maize -Glucosidase*
-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
-glucosidase aggregating factor (BGAF) is responsible for the null
phenotype, and it specifically interacts with maize -glucosidases
and forms large insoluble aggregates. To understand the mechanism of
the -glucosidase-BGAF interaction, we constructed chimeric enzymes
by domain swapping between the maize -glucosidase isozymes Glu1 and
Gu2, to which BGAF binds, and the sorghum -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 (Glu50-Val145) and an extreme
C-terminal region (Phe466-Ala512) 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 reverse transcriptase-polymerase chain reaction, expressed it in
Escherichia coli, and showed that it encodes a protein
whose binding and immunological properties are identical to the native
BGAF isolated from maize tissues. A data base search revealed that BGAF
is a member of the jasmonite-induced protein family. Interestingly, the
deduced BGAF sequence contained an octapeptide sequence
(G(P/R)WGGSGG) repeated twice. Each of these repeat units is
postulated to be involved in forming a site for binding to maize
-glucosidases and thus provides a plausible explanation for the
divalent function of BGAF predicted from binding assays.
*
This research was supported by Grant MCB-9906698 from the
National Science Foundation, by Jeffress Foundation Grant J-377, and by
a Sigma Xi grant in aid of research (to D. J. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Tel.: 540-231-8951;
Fax: 540-231-9307; E-mail: aevatan@vt.edu.
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