This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 148/3/1412    most recent pp.108.128413v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (5) Citing Articles via Google Scholar Google Scholar Articles by Ogawa, T. Articles by Shigeoka, S. Search for Related Content PubMed PubMed Citation Articles by Ogawa, T. Articles by Shigeoka, S. Agricola Articles by Ogawa, T. Articles by Shigeoka, S.

CELL BIOLOGY AND SIGNAL TRANSDUCTION

Molecular Characterization of Organelle-Type Nudix Hydrolases in Arabidopsis^1,[W]

Department of Advanced Bioscience, Faculty of Agriculture, Kinki University, Nara 631–8505, Japan (T.O., H.M., K.I., D.I., N.T., S.S.); and Department of Food and Nutritional Science, College of Bioscience and Biotechnology, Chubu University, Kasugai, Aichi 487–8501, Japan (K.Y.)

Nudix (for nucleoside diphosphates linked to some moiety X) hydrolases act to hydrolyze ribonucleoside and deoxyribonucleoside triphosphates, nucleotide sugars, coenzymes, or dinucleoside polyphosphates. Arabidopsis (Arabidopsis thaliana) contains 27 genes encoding Nudix hydrolase homologues (AtNUDX1 to -27) with a predicted distribution in the cytosol, mitochondria, and chloroplasts. Previously, cytosolic Nudix hydrolases (AtNUDX1 to -11 and -25) were characterized. Here, we conducted a characterization of organelle-type AtNUDX proteins (AtNUDX12 to -24, -26, and -27). AtNUDX14 showed pyrophosphohydrolase activity toward both ADP-ribose and ADP-glucose, although its K_m value was approximately 100-fold lower for ADP-ribose (13.0 ± 0.7 µM) than for ADP-glucose (1,235 ± 65 µM). AtNUDX15 hydrolyzed not only reduced coenzyme A (118.7 ± 3.4 µM) but also a wide range of its derivatives. AtNUDX19 showed pyrophosphohydrolase activity toward both NADH (335.3 ± 5.4 µM) and NADPH (36.9 ± 3.5 µM). AtNUDX23 had flavin adenine dinucleotide pyrophosphohydrolase activity (9.1 ± 0.9 µM). Both AtNUDX26 and AtNUDX27 hydrolyzed diadenosine polyphosphates (n = 4–5). A confocal microscopic analysis using a green fluorescent protein fusion protein showed that AtNUDX15 is distributed in mitochondria and AtNUDX14 -19, -23, -26, and -27 are distributed in chloroplasts. These AtNUDX mRNAs were detected ubiquitously in various Arabidopsis tissues. The T-DNA insertion mutants of AtNUDX13, -14, -15, -19, -20, -21, -25, -26, and -27 did not exhibit any phenotypical differences under normal growth conditions. These results suggest that Nudix hydrolases in Arabidopsis control a variety of metabolites and are pertinent to a wide range of physiological processes.

² These authors contributed equally to the article.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Shigeru Shigeoka (shigeoka{at}nara.kindai.ac.jp).

^[W] The online version of this article contains Web-only data.

www.plantphysiol.org/cgi/doi/10.1104/pp.108.128413

^* Corresponding author; e-mail shigeoka{at}nara.kindai.ac.jp.

Received August 26, 2008; accepted September 22, 2008; published September 24, 2008.

This article has been cited by other articles:

				K. Ishikawa, T. Ogawa, E. Hirosue, Y. Nakayama, K. Harada, E. Fukusaki, K. Yoshimura, and S. Shigeoka Modulation of the Poly(ADP-ribosyl)ation Reaction via the Arabidopsis ADP-Ribose/NADH Pyrophosphohydrolase, AtNUDX7, Is Involved in the Response to Oxidative Stress Plant Physiology, October 1, 2009; 151(2): 741 - 754. [Abstract] [Full Text] [PDF]

				S.-n. Hashida, H. Takahashi, and H. Uchimiya The role of NAD biosynthesis in plant development and stress responses Ann. Bot., April 1, 2009; 103(6): 819 - 824. [Abstract] [Full Text] [PDF]