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Titolo:
Cloning of chlorophyllase, the key enzyme in chlorophyll degradation: Finding of a lipase motif and the induction by methyl jasmonate
Autore:
Tsuchiya, T; Ohta, H; Okawa, K; Iwamatsu, A; Shimada, H; Masuda, T; Takamiya, K;
Indirizzi:
Tokyo Inst Technol, Fac Biosci & Biotechnol, Dept Biol Sci, Midori Ku, Yokohama, Kanagawa 2268501, Japan Tokyo Inst Technol Yokohama Kanagawa Japan 2268501 anagawa 2268501, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan 2360004 agawa 2360004, Japan
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 26, volume: 96, anno: 1999,
pagine: 15362 - 15367
SICI:
0027-8424(199912)96:26<15362:COCTKE>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHENOPODIUM-ALBUM; CHLOROPLAST MEMBRANES; PHYTOTOXIN CORONATINE; BARLEY LEAVES; PLANT-CELLS; IDENTIFICATION; PURIFICATION; ARABIDOPSIS; PROTEINS; VACUOLES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Takamiya, K Tokyo Inst Technol, Fac Biosci & Biotechnol, Dept Biol Sci, Midori Ku, 4259 Nagatsuta, Yokohama, Kanagawa 2268501, Japan Tokyo Inst Technol 4259 Nagatsuta Yokohama Kanagawa Japan 2268501
Citazione:
T. Tsuchiya et al., "Cloning of chlorophyllase, the key enzyme in chlorophyll degradation: Finding of a lipase motif and the induction by methyl jasmonate", P NAS US, 96(26), 1999, pp. 15362-15367

Abstract

Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol. In the present study, we isolated the Chlase cDNA. We synthesized degenerate oligo DNA probes based on the internal amino acid sequences of purified Chlase from Chenopodium album, screened the C. album cDNA library, and cloned a cDNA (CaCLH, C. album chlorophyll-chlorophyllido hydrolase). The deduced amino acid sequence (347 aa residues) had a lipase motif overlapping with an ATP/GTP-binding motif (P-loop), CaCLH possibly was localized in the extraplastidic part of the cell, because a putative signal sequence for endoplasmic reticulum is at the N terminus. The amino acid sequence shared 37% identity with a function-unknown gene whose mRNA is inducibleby coronatine and methyl jasmonate (MeJA) in Arabidopsis thaliana (AtCLH1). We expressed the gene products of AtCLH1 and of CaCLH in Escherichia coil, and they similarly exhibited Chlase activity. Moreover, we isolated another full-length cDNA based on an Arabidopsis genomic fragment and expressed it in E. coil, demonstrating the presence of the second Arabidopsis CLH gene (AtCLH2). No typical feature of signal sequence was identified in AtCLH1,whereas AtCLH2 had a typical signal sequence for chloroplast. AtCLH1 mRNA was induced rapidly by a treatment of MeJA, which is known to promote senescence and chi degradation in plants, and a high mRNA level was maintained up to 9 h. AtCLH2, however, did not respond to MeJA.

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Documento generato il 15/01/21 alle ore 23:04:17