Journal Article

An Isozyme of Betaine Aldehyde Dehydrogenase in Barley

Toshihide Nakamura, Mika Nomura, Hitoshi Mori, Andre T. Jagendorf, Akihiro Ueda and Tetsuko Takabe

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 42, issue 10, pages 1088-1092
Published in print October 2001 | ISSN: 0032-0781
Published online October 2001 | e-ISSN: 1471-9053 | DOI:
An Isozyme of Betaine Aldehyde Dehydrogenase in

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry


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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 was more 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.

Keywords: Key words: Barley — Betaine aldehyde dehydrogenase (EC — Gly betaine —Salinity stress.; Abbreviations: BADH, betaine aldehyde dehydrogenase; ABA, abscisic acid; PEG, polyethylene glycol.

Journal Article.  3106 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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