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J. Biol. Chem., Vol. 275, Issue 45, 35122-35128, November 10, 2000
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From the We report on the molecular, biochemical, and
functional characterization of Cucurbita maxima phloem
serpin-1 (CmPS-1), a novel 42-kDa serine proteinase inhibitor that is
developmentally regulated and has anti-elastase properties. CmPS-1 was
purified to near homogeneity from C. maxima (pumpkin)
phloem exudate and, based on microsequence analysis, the cDNA
encoding CmPS-1 was cloned. The association rate constant
(ka) of phloem-purified and recombinant
His6-tagged CmPS-1 for elastase was 3.5 ± 1.6 × 105 and 2.7 ± 0.4 × 105
M The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF284038 (CmPS-1).
Characterization of Cucurbita maxima Phloem Serpin-1
(CmPS-1)
A DEVELOPMENTALLY REGULATED ELASTASE INHIBITOR*
,,§,
,**,,,
Section of Plant Biology, Division of
Biological Sciences and the ¶ Department of Entomolgy, College of
Agriculture and Environmental Sciences, University of California,
Davis, California 95616
1 s1,
respectively. The fraction of complex-forming CmPS-1, Xinh, was estimated at 79%. CmPS-1 displayed no detectable inhibitory properties against chymotrypsin, trypsin, or thrombin. The elastase cleavage sites within the reactive center loop of CmPS-1 were determined to be Val347-Gly348 and
Val350-Ser351 with a 3:2 molar ratio. In
vivo feeding assays conducted with the piercing-sucking aphid,
Myzus persicae, established a close correlation between the
developmentally regulated increase in CmPS-1 within the phloem sap and
the reduced ability of these insects to survive and reproduce on
C. maxima. However, in vitro feeding
experiments, using purified phloem CmPS-1, failed to demonstrate a
direct effect on aphid survival. Likely roles of this novel phloem
serpin in defense against insects/pathogens are discussed.
*
This work was supported by U. S. Department of Energy
Biosciences Grant DE-FG03-94ER20134 (to W. J. L.).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.
On sabbatical leave from: Plant Sciences Dept., University of
Rhode Island, Kingston, RI 02881-0804.
**
Present address: Dept. de Biotecnología y
Bioingeniería, CINVESTAV-IPN, Ave. I.P.N. 2508, Zacatenco,
México D.F. 07360.
To whom correspondence should be addressed: Section of Plant
Biology, Div. of Biological Sciences, University of California, One
Shields Ave., Davis, CA 95616. Tel.: 530-752-1093; Fax: 530-752-5410; E-mail: wjlucas@ucdavis.edu.
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