Characterization of nuclear factors for elicitor-mediated activation of the promoter of the pea phenylalanine ammonia-lyase gene 1

Hisaharu Kato, Manabu Wada, Keiko Muraya, Kamal Malik, Tomonori Shiraishi, Yuki Ichinose, Tetsuji Yamada

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

The nuclear factors presumably associated with the activation of the gene encoding phenylalanine ammonia-lyase by a fungal elicitor were characterized in pea (Pisum sativum L.) epicotyls. The TATA-proximal region was dissected and putative cis-regulatory elements in the promoter of pea phenylalanine ammonia-lyase gene 1 were examined by gel-mobility shift and in vitro footprinting analyses. Specific binding of the nuclear factors to the promoter-proximal regions of pea phenylalanine ammonia-lyase gene 1 associated with elicitor-mediated activation was detected at a region containing consensus sequence motifs of boxes 2 and 4 and other AT-rich sequences. The analyses of DNA fragments containing the deleted promoter regions suggested that a residue from -183 to -173 (ATTAGTAAGTGAT) was essential for a maximal activity of forming low-mobility complex (LMC) in the gel-mobility shift assay, and synthetic oligonucleotides confirmed the presence of at least one nuclear component associated with the formation of an active LMC. Competition experiments and treatment with Hoechst 33258 provided direct evidence that the formation of LMC with the promoter fragments from genes encoding phenylalanine ammonia-lyase and chalcone synthase in pea contained one or more of the same proteins that recognize AT-rich sequence motifs for binding. It also suggests that common high-mobility group-like proteins might be involved in the regulation of elicitor-inducible genes in pea.

Original languageEnglish
Pages (from-to)129-139
Number of pages11
JournalPlant Physiology
Volume108
Issue number1
Publication statusPublished - May 1995

Fingerprint

Phenylalanine Ammonia-Lyase
Peas
phenylalanine ammonia-lyase
peas
promoter regions
AT Rich Sequence
Genes
genes
Genetic Promoter Regions
gels
Gels
regulatory sequences
naringenin-chalcone synthase
gene activation
epicotyls
High Mobility Group Proteins
consensus sequence
Bisbenzimidazole
oligonucleotides
Pisum sativum

ASJC Scopus subject areas

  • Plant Science

Cite this

Characterization of nuclear factors for elicitor-mediated activation of the promoter of the pea phenylalanine ammonia-lyase gene 1. / Kato, Hisaharu; Wada, Manabu; Muraya, Keiko; Malik, Kamal; Shiraishi, Tomonori; Ichinose, Yuki; Yamada, Tetsuji.

In: Plant Physiology, Vol. 108, No. 1, 05.1995, p. 129-139.

Research output: Contribution to journalArticle

Kato, Hisaharu ; Wada, Manabu ; Muraya, Keiko ; Malik, Kamal ; Shiraishi, Tomonori ; Ichinose, Yuki ; Yamada, Tetsuji. / Characterization of nuclear factors for elicitor-mediated activation of the promoter of the pea phenylalanine ammonia-lyase gene 1. In: Plant Physiology. 1995 ; Vol. 108, No. 1. pp. 129-139.
@article{76be78e9d43b45c09271bfbf1fc75541,
title = "Characterization of nuclear factors for elicitor-mediated activation of the promoter of the pea phenylalanine ammonia-lyase gene 1",
abstract = "The nuclear factors presumably associated with the activation of the gene encoding phenylalanine ammonia-lyase by a fungal elicitor were characterized in pea (Pisum sativum L.) epicotyls. The TATA-proximal region was dissected and putative cis-regulatory elements in the promoter of pea phenylalanine ammonia-lyase gene 1 were examined by gel-mobility shift and in vitro footprinting analyses. Specific binding of the nuclear factors to the promoter-proximal regions of pea phenylalanine ammonia-lyase gene 1 associated with elicitor-mediated activation was detected at a region containing consensus sequence motifs of boxes 2 and 4 and other AT-rich sequences. The analyses of DNA fragments containing the deleted promoter regions suggested that a residue from -183 to -173 (ATTAGTAAGTGAT) was essential for a maximal activity of forming low-mobility complex (LMC) in the gel-mobility shift assay, and synthetic oligonucleotides confirmed the presence of at least one nuclear component associated with the formation of an active LMC. Competition experiments and treatment with Hoechst 33258 provided direct evidence that the formation of LMC with the promoter fragments from genes encoding phenylalanine ammonia-lyase and chalcone synthase in pea contained one or more of the same proteins that recognize AT-rich sequence motifs for binding. It also suggests that common high-mobility group-like proteins might be involved in the regulation of elicitor-inducible genes in pea.",
author = "Hisaharu Kato and Manabu Wada and Keiko Muraya and Kamal Malik and Tomonori Shiraishi and Yuki Ichinose and Tetsuji Yamada",
year = "1995",
month = "5",
language = "English",
volume = "108",
pages = "129--139",
journal = "Plant Physiology",
issn = "0032-0889",
publisher = "American Society of Plant Biologists",
number = "1",

}

TY - JOUR

T1 - Characterization of nuclear factors for elicitor-mediated activation of the promoter of the pea phenylalanine ammonia-lyase gene 1

AU - Kato, Hisaharu

AU - Wada, Manabu

AU - Muraya, Keiko

AU - Malik, Kamal

AU - Shiraishi, Tomonori

AU - Ichinose, Yuki

AU - Yamada, Tetsuji

PY - 1995/5

Y1 - 1995/5

N2 - The nuclear factors presumably associated with the activation of the gene encoding phenylalanine ammonia-lyase by a fungal elicitor were characterized in pea (Pisum sativum L.) epicotyls. The TATA-proximal region was dissected and putative cis-regulatory elements in the promoter of pea phenylalanine ammonia-lyase gene 1 were examined by gel-mobility shift and in vitro footprinting analyses. Specific binding of the nuclear factors to the promoter-proximal regions of pea phenylalanine ammonia-lyase gene 1 associated with elicitor-mediated activation was detected at a region containing consensus sequence motifs of boxes 2 and 4 and other AT-rich sequences. The analyses of DNA fragments containing the deleted promoter regions suggested that a residue from -183 to -173 (ATTAGTAAGTGAT) was essential for a maximal activity of forming low-mobility complex (LMC) in the gel-mobility shift assay, and synthetic oligonucleotides confirmed the presence of at least one nuclear component associated with the formation of an active LMC. Competition experiments and treatment with Hoechst 33258 provided direct evidence that the formation of LMC with the promoter fragments from genes encoding phenylalanine ammonia-lyase and chalcone synthase in pea contained one or more of the same proteins that recognize AT-rich sequence motifs for binding. It also suggests that common high-mobility group-like proteins might be involved in the regulation of elicitor-inducible genes in pea.

AB - The nuclear factors presumably associated with the activation of the gene encoding phenylalanine ammonia-lyase by a fungal elicitor were characterized in pea (Pisum sativum L.) epicotyls. The TATA-proximal region was dissected and putative cis-regulatory elements in the promoter of pea phenylalanine ammonia-lyase gene 1 were examined by gel-mobility shift and in vitro footprinting analyses. Specific binding of the nuclear factors to the promoter-proximal regions of pea phenylalanine ammonia-lyase gene 1 associated with elicitor-mediated activation was detected at a region containing consensus sequence motifs of boxes 2 and 4 and other AT-rich sequences. The analyses of DNA fragments containing the deleted promoter regions suggested that a residue from -183 to -173 (ATTAGTAAGTGAT) was essential for a maximal activity of forming low-mobility complex (LMC) in the gel-mobility shift assay, and synthetic oligonucleotides confirmed the presence of at least one nuclear component associated with the formation of an active LMC. Competition experiments and treatment with Hoechst 33258 provided direct evidence that the formation of LMC with the promoter fragments from genes encoding phenylalanine ammonia-lyase and chalcone synthase in pea contained one or more of the same proteins that recognize AT-rich sequence motifs for binding. It also suggests that common high-mobility group-like proteins might be involved in the regulation of elicitor-inducible genes in pea.

UR - http://www.scopus.com/inward/record.url?scp=0029294567&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029294567&partnerID=8YFLogxK

M3 - Article

C2 - 7540308

AN - SCOPUS:0029294567

VL - 108

SP - 129

EP - 139

JO - Plant Physiology

JF - Plant Physiology

SN - 0032-0889

IS - 1

ER -