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Science 301 (5633): 653-657
Copyright © 2003 by the American Association for the Advancement of Science
Genome-Wide Insertional Mutagenesis of Arabidopsis thaliana
José M. Alonso,1*
Anna N. Stepanova,1*
Thomas J. Leisse,1
Christopher J. Kim,1
Huaming Chen,1
Paul Shinn,1
Denise K. Stevenson,1
Justin Zimmerman,1
Pascual Barajas,1
Rosa Cheuk,1
Carmelita Gadrinab,1
Collen Heller,1
Albert Jeske,1
Eric Koesema,1
Cristina C. Meyers,1
Holly Parker,1
Lance Prednis,1
Yasser Ansari,1
Nathan Choy,1
Hashim Deen,1
Michael Geralt,1
Nisha Hazari,1
Emily Hom,1
Meagan Karnes,1
Celene Mulholland,1
Ral Ndubaku,1
Ian Schmidt,1
Plinio Guzman,1
Laura Aguilar-Henonin,1
Markus Schmid,1
Detlef Weigel,1
David E. Carter,2
Trudy Marchand,2
Eddy Risseeuw,2
Debra Brogden,2
Albana Zeko,2
William L. Crosby,2
Charles C. Berry,3
Joseph R. Ecker1
Abstract:
Over 225,000 independent Agrobacterium transferred DNA (T-DNA) insertion events in the genome of the reference plant Arabidopsis thaliana have been created that represent near saturation of the gene space. The precise locations were determined for more than 88,000 T-DNA insertions, which resulted in the identification of mutations in more than 21,700 of the 29,454 predicted Arabidopsis genes. Genome-wide analysis of the distribution of integration events revealed the existence of a large integration site bias at both the chromosome and gene levels. Insertion mutations were identified in genes that are regulated in response to the plant hormone ethylene.
1 Genomic Analysis Laboratory, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
2 National Research Council Plant Biotechnology Institute, Saskatoon, SK, S7N 0W9 Canada.
3 Department of Family/Preventive Medicine, University of California, San Diego, CA 92093, USA.
* Present address: Department of Genetics, Box 7614, North Carolina State University, Raleigh, NC 27695, USA.
Present address: Department of Molecular Biology, Max Planck Institute for Developmental Biology, Spemannstrasse 37-39, D-72076 Tübingen, Germany.
To whom correspondence should be addressed. E-mail: ecker{at}salk.edu
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- Two Interacting Proteins Are Necessary for the Editing of the NdhD-1 Site in Arabidopsis Plastids.
- C. Boussardon, V. Salone, A. Avon, R. Berthome, K. Hammani, K. Okuda, T. Shikanai, I. Small, and C. Lurin (2012)
PLANT CELL
24, 3684-3694
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- A Systems Biology View of Responses to Lignin Biosynthesis Perturbations in Arabidopsis.
- R. Vanholme, V. Storme, B. Vanholme, L. Sundin, J. H. Christensen, G. Goeminne, C. Halpin, A. Rohde, K. Morreel, and W. Boerjan (2012)
PLANT CELL
24, 3506-3529
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- IAA-Ala Resistant3, an Evolutionarily Conserved Target of miR167, Mediates Arabidopsis Root Architecture Changes during High Osmotic Stress.
- N. Kinoshita, H. Wang, H. Kasahara, J. Liu, C. MacPherson, Y. Machida, Y. Kamiya, M. A. Hannah, and N.-H. Chua (2012)
PLANT CELL
24, 3590-3602
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- Characterization of SOC1's Central Role in Flowering by the Identification of Its Upstream and Downstream Regulators.
- R. G. H. Immink, D. Pose, S. Ferrario, F. Ott, K. Kaufmann, F. L. Valentim, S. de Folter, F. van der Wal, A. D. J. van Dijk, M. Schmid, et al. (2012)
Plant Physiology
160, 433-449
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- The Lateral Organ Boundaries Domain Transcription Factor LBD20 Functions in Fusarium Wilt Susceptibility and Jasmonate Signaling in Arabidopsis.
- L. F. Thatcher, J. J. Powell, E. A. B. Aitken, K. Kazan, and J. M. Manners (2012)
Plant Physiology
160, 407-418
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- Identification of an Arabidopsis Fatty Alcohol:Caffeoyl-Coenzyme A Acyltransferase Required for the Synthesis of Alkyl Hydroxycinnamates in Root Waxes.
- D. K. Kosma, I. Molina, J. B. Ohlrogge, and M. Pollard (2012)
Plant Physiology
160, 237-248
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- The Subcellular Localization of Tubby-Like Proteins and Participation in Stress Signaling and Root Colonization by the Mutualist Piriformospora indica.
- M. U. Reitz, J. K. Bissue, K. Zocher, A. Attard, R. Huckelhoven, K. Becker, J. Imani, R. Eichmann, and P. Schafer (2012)
Plant Physiology
160, 349-364
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- The Light-Response BTB1 and BTB2 Proteins Assemble Nuclear Ubiquitin Ligases That Modify Phytochrome B and D Signaling in Arabidopsis.
- M. J. Christians, D. J. Gingerich, Z. Hua, T. D. Lauer, and R. D. Vierstra (2012)
Plant Physiology
160, 118-134
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- Assembly of an Evolutionarily New Pathway for {alpha}-Pyrone Biosynthesis in Arabidopsis.
- J.-K. Weng, Y. Li, H. Mo, and C. Chapple (2012)
Science
337, 960-964
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- Incidence of Genome Structure, DNA Asymmetry, and Cell Physiology on T-DNA Integration in Chromosomes of the Phytopathogenic Fungus Leptosphaeria maculans.
- S. Bourras, M. Meyer, J. Grandaubert, N. Lapalu, I. Fudal, J. Linglin, B. Ollivier, F. Blaise, M.-H. Balesdent, and T. Rouxel (2012)
g3
2, 891-904
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- Identification of Natural Diterpenes that Inhibit Bacterial Wilt Disease in Tobacco, Tomato and Arabidopsis.
- S. Seo, K. Gomi, H. Kaku, H. Abe, H. Seto, S. Nakatsu, M. Neya, M. Kobayashi, K. Nakaho, Y. Ichinose, et al. (2012)
Plant Cell Physiol.
53, 1432-1444
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- Arabidopsis GROWTH-REGULATING FACTOR7 Functions as a Transcriptional Repressor of Abscisic Acid- and Osmotic Stress-Responsive Genes, Including DREB2A.
- J.-S. Kim, J. Mizoi, S. Kidokoro, K. Maruyama, J. Nakajima, K. Nakashima, N. Mitsuda, Y. Takiguchi, M. Ohme-Takagi, Y. Kondou, et al. (2012)
PLANT CELL
24, 3393-3405
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- RDR1 and SGS3, Components of RNA-Mediated Gene Silencing, Are Required for the Regulation of Cuticular Wax Biosynthesis in Developing Inflorescence Stems of Arabidopsis.
- P. Lam, L. Zhao, H. E. McFarlane, M. Aiga, V. Lam, T. S. Hooker, and L. Kunst (2012)
Plant Physiology
159, 1385-1395
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- ASPARTATE OXIDASE Plays an Important Role in Arabidopsis Stomatal Immunity.
- A. P. Macho, F. Boutrot, J. P. Rathjen, and C. Zipfel (2012)
Plant Physiology
159, 1845-1856
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- A Medicago truncatula Tobacco Retrotransposon Insertion Mutant Collection with Defects in Nodule Development and Symbiotic Nitrogen Fixation.
- C. I. Pislariu, J. D. Murray, J. Wen, V. Cosson, R. R. D. Muni, M. Wang, V. A. Benedito, A. Andriankaja, X. Cheng, I. T. Jerez, et al. (2012)
Plant Physiology
159, 1686-1699
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- The Arabidopsis Homolog of the Mammalian OS-9 Protein Plays a Key Role in the Endoplasmic Reticulum-Associated Degradation of Misfolded Receptor-Like Kinases.
- W. Su, Y. Liu, Y. Xia, Z. Hong, and J. Li (2012)
Mol Plant
5, 929-940
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