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Titolo:
An isozyme of betaine aldehyde dehydrogenase in barley
Autore:
Nakamura, T; Nomura, M; Mori, H; Jagendorf, AT; Ueda, A; Takabe, T;
Indirizzi:
Nagoya Univ, Grad Sch Bioagr Sci, Chikusa Ku, Nagoya, Aichi 4648601, JapanNagoya Univ Nagoya Aichi Japan 4648601 a Ku, Nagoya, Aichi 4648601, Japan Kagawa Univ, Fac Agr, Kita Ku, Kagawa 7610795, Japan Kagawa Univ Kagawa Japan 7610795 Fac Agr, Kita Ku, Kagawa 7610795, Japan Cornell Univ, Plant Biol Sect, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA 14853 v, Plant Biol Sect, Ithaca, NY 14853 USA
Titolo Testata:
PLANT AND CELL PHYSIOLOGY
fascicolo: 10, volume: 42, anno: 2001,
pagine: 1088 - 1092
SICI:
0032-0781(200110)42:10<1088:AIOBAD>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHOLINE MONOOXYGENASE; EFFICIENTLY CATALYZES; MOLECULAR-CLONING; SPINACH LEAVES; OSMOTIC-STRESS; CDNA CLONING; SUGAR-BEET; EXPRESSION; PLANTS; GLYCINEBETAINE;
Keywords:
barley; betaine aldehyde dehydrogenase (EC 1.2.1.8); gly betaine; salinity stress;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Takabe, T Nagoya Univ, Grad Sch Bioagr Sci, Chikusa Ku, Nagoya, Aichi 4648601, Japan Nagoya Univ Nagoya Aichi Japan 4648601 ya, Aichi 4648601, Japan
Citazione:
T. Nakamura et al., "An isozyme of betaine aldehyde dehydrogenase in barley", PLANT CEL P, 42(10), 2001, pp. 1088-1092

Abstract

Betaine aldehyde dehydrogenase (BADH) is an important enzyme for Gly betaine synthesis. We isolated two types of BADH cDNAs (BBD1 and BBD2) from barley. As BBD1 contained the signal sequence (SKL) targeting to microbodies. BBD2 was more similar to previously reported genes coding for BADH in dicotyledons (chloroplast type) than those in monocotyledons (microbody type). The two barley BADH genes showed different expression patterns. The BBD1 transcript was more abundant in roots than leaves and was induced to higher levels by salt, drought and abscisic acid (ABA) treatment. BBD2 transcript wasmore abundant in leaves and induced by salt, drought, PEG and ABA treatment. To understand the processing of these BADH proteins, we partially purified both enzymes and determined their N-terminal sequences. Based on comparisons of the N-terminal sequences to their deduced amino acid sequence, neither BBD1 nor BBD2 is processed at the N-terminus. These results suggest that BBD2 codes for a new type of BADH, which is not localized in either chloroplasts or mitochondria.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 06:02:46