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Title: cDNA encoding a polypeptide including a hevein sequence

Abstract

A cDNA clone (HEV1) encoding hevein was isolated via polymerase chain reaction (PCR) using mixed oligonucleotides corresponding to two regions of hevein as primers and a Hevea brasiliensis latex cDNA library as a template. HEV1 is 1018 nucleotides long and includes an open reading frame of 204 amino acids. The deduced amino acid sequence contains a putative signal sequence of 17 amino acid residues followed by a 187 amino acid polypeptide. The amino-terminal region (43 amino acids) is identical to hevein and shows homology to several chitin-binding proteins and to the amino-termini of wound-induced genes in potato and poplar. The carboxyl-terminal portion of the polypeptide (144 amino acids) is 74--79% homologous to the carboxyl-terminal region of wound-inducible genes of potato. Wounding, as well as application of the plant hormones abscisic acid and ethylene, resulted in accumulation of hevein transcripts in leaves, stems and latex, but not in roots, as shown by using the cDNA as a probe. A fusion protein was produced in E. coli from the protein of the present invention and maltose binding protein produced by the E. coli. 12 figs.

Inventors:
; ; ;
Issue Date:
Research Org.:
Michigan State Univ., East Lansing, MI (United States)
Sponsoring Org.:
USDOE, Washington, DC (United States)
OSTI Identifier:
350323
Patent Number(s):
5,900,480
Application Number:
PAN: 7-888,366
Assignee:
Michigan State Univ., East Lansing, MI (United States) PTO; SCA: 550200; PA: EDB-99:064282; SN: 99002098254
DOE Contract Number:  
AC02-76ER01338
Resource Type:
Patent
Resource Relation:
Other Information: PBD: 4 May 1999
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; DNA-CLONING; POLYMERASE CHAIN REACTION; POLYPEPTIDES; AMINO ACID SEQUENCE; GENES

Citation Formats

Raikhel, N.V., Broekaert, W.F., Chua, N.H., and Kush, A. cDNA encoding a polypeptide including a hevein sequence. United States: N. p., 1999. Web.
Raikhel, N.V., Broekaert, W.F., Chua, N.H., & Kush, A. cDNA encoding a polypeptide including a hevein sequence. United States.
Raikhel, N.V., Broekaert, W.F., Chua, N.H., and Kush, A. Tue . "cDNA encoding a polypeptide including a hevein sequence". United States.
@article{osti_350323,
title = {cDNA encoding a polypeptide including a hevein sequence},
author = {Raikhel, N.V. and Broekaert, W.F. and Chua, N.H. and Kush, A.},
abstractNote = {A cDNA clone (HEV1) encoding hevein was isolated via polymerase chain reaction (PCR) using mixed oligonucleotides corresponding to two regions of hevein as primers and a Hevea brasiliensis latex cDNA library as a template. HEV1 is 1018 nucleotides long and includes an open reading frame of 204 amino acids. The deduced amino acid sequence contains a putative signal sequence of 17 amino acid residues followed by a 187 amino acid polypeptide. The amino-terminal region (43 amino acids) is identical to hevein and shows homology to several chitin-binding proteins and to the amino-termini of wound-induced genes in potato and poplar. The carboxyl-terminal portion of the polypeptide (144 amino acids) is 74--79% homologous to the carboxyl-terminal region of wound-inducible genes of potato. Wounding, as well as application of the plant hormones abscisic acid and ethylene, resulted in accumulation of hevein transcripts in leaves, stems and latex, but not in roots, as shown by using the cDNA as a probe. A fusion protein was produced in E. coli from the protein of the present invention and maltose binding protein produced by the E. coli. 12 figs.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {1999},
month = {5}
}