Structure and characterization of a cDNA clone for phenylalanine ammonia-lyase from cut-injured roots of sweet potato
Abstract
A cDNA clone for phenylalanine ammonia-lyase (PAL) induced in wounded sweet potato (Ipomoea batatas Lam.) root was obtained by immunoscreening a cDNA library. The protein produced in Escherichia coli cells containing the plasmid pPAL02 was indistinguishable from sweet potato PAL as judged by Ouchterlony double diffusion assays. The M{sub r} of its subunit was 77,000. The cells converted ({sup 14}C)-L-phenylalanine into ({sup 14}C)-t-cinnamic acid and PAL activity was detected in the homogenate of the cells. The activity was dependent on the presence of the pPAL02 plasmid DNA. The nucleotide sequence of the cDNA contained a 2,121-base pair (bp) open-reading frame capable of coding for a polypeptide with 707 amino acids (M{sub r} 77,137), a 22-bp 5{prime}-noncoding region and a 207-bp 3{prime}-noncoding region. The results suggest that the insert DNA fully encoded the amino acid sequence for sweet potato PAL that is induced by wounding. Comparison of the deduced amino acid sequence with that of a PAL cDNA fragment from Phaseolus vulgaris revealed 78.9% homology. The sequence from amino acid residues 258 to 494 was highly conserved, showing 90.7% homology.
- Authors:
-
- National Institute of Agro-Environmental Sciences, Ibaraki (Japan) Univ. of Tokyo (Japan)
- Publication Date:
- OSTI Identifier:
- 6874152
- Resource Type:
- Journal Article
- Journal Name:
- Plant Physiology; (USA)
- Additional Journal Information:
- Journal Volume: 90:4; Journal ID: ISSN 0032-0889
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; LYASES; DNA-CLONING; POTATOES; INJURIES; AMINO ACID SEQUENCE; CARBON 14 COMPOUNDS; CHEMICAL COMPOSITION; CINNAMIC ACID; COMPARATIVE EVALUATIONS; ENZYME ACTIVITY; MOLECULAR STRUCTURE; PHASEOLUS; PHENYLALANINE; TRACER TECHNIQUES; AMINO ACIDS; CARBOXYLIC ACIDS; CLONING; DNA HYBRIDIZATION; ENZYMES; FOOD; HYBRIDIZATION; ISOTOPE APPLICATIONS; LABELLED COMPOUNDS; LEGUMINOSAE; MAGNOLIOPHYTA; MAGNOLIOPSIDA; MONOCARBOXYLIC ACIDS; ORGANIC ACIDS; ORGANIC COMPOUNDS; PLANTS; TUBERS; VEGETABLES; 550201* - Biochemistry- Tracer Techniques
Citation Formats
Tanaka, Yoshiyuki, Matsuoka, Makoto, Yamanoto, Naoki, Ohashi, Yuko, Kano-Murakami, Yuriko, and Ozeki, Yoshihiro. Structure and characterization of a cDNA clone for phenylalanine ammonia-lyase from cut-injured roots of sweet potato. United States: N. p., 1989.
Web. doi:10.1104/pp.90.4.1403.
Tanaka, Yoshiyuki, Matsuoka, Makoto, Yamanoto, Naoki, Ohashi, Yuko, Kano-Murakami, Yuriko, & Ozeki, Yoshihiro. Structure and characterization of a cDNA clone for phenylalanine ammonia-lyase from cut-injured roots of sweet potato. United States. https://doi.org/10.1104/pp.90.4.1403
Tanaka, Yoshiyuki, Matsuoka, Makoto, Yamanoto, Naoki, Ohashi, Yuko, Kano-Murakami, Yuriko, and Ozeki, Yoshihiro. 1989.
"Structure and characterization of a cDNA clone for phenylalanine ammonia-lyase from cut-injured roots of sweet potato". United States. https://doi.org/10.1104/pp.90.4.1403.
@article{osti_6874152,
title = {Structure and characterization of a cDNA clone for phenylalanine ammonia-lyase from cut-injured roots of sweet potato},
author = {Tanaka, Yoshiyuki and Matsuoka, Makoto and Yamanoto, Naoki and Ohashi, Yuko and Kano-Murakami, Yuriko and Ozeki, Yoshihiro},
abstractNote = {A cDNA clone for phenylalanine ammonia-lyase (PAL) induced in wounded sweet potato (Ipomoea batatas Lam.) root was obtained by immunoscreening a cDNA library. The protein produced in Escherichia coli cells containing the plasmid pPAL02 was indistinguishable from sweet potato PAL as judged by Ouchterlony double diffusion assays. The M{sub r} of its subunit was 77,000. The cells converted ({sup 14}C)-L-phenylalanine into ({sup 14}C)-t-cinnamic acid and PAL activity was detected in the homogenate of the cells. The activity was dependent on the presence of the pPAL02 plasmid DNA. The nucleotide sequence of the cDNA contained a 2,121-base pair (bp) open-reading frame capable of coding for a polypeptide with 707 amino acids (M{sub r} 77,137), a 22-bp 5{prime}-noncoding region and a 207-bp 3{prime}-noncoding region. The results suggest that the insert DNA fully encoded the amino acid sequence for sweet potato PAL that is induced by wounding. Comparison of the deduced amino acid sequence with that of a PAL cDNA fragment from Phaseolus vulgaris revealed 78.9% homology. The sequence from amino acid residues 258 to 494 was highly conserved, showing 90.7% homology.},
doi = {10.1104/pp.90.4.1403},
url = {https://www.osti.gov/biblio/6874152},
journal = {Plant Physiology; (USA)},
issn = {0032-0889},
number = ,
volume = 90:4,
place = {United States},
year = {Tue Aug 01 00:00:00 EDT 1989},
month = {Tue Aug 01 00:00:00 EDT 1989}
}