Browse > Article
http://dx.doi.org/10.5483/BMBRep.2011.44.10.680

Comprehensive analysis of AHL homologous genes encoding AT-hook motif nuclear localized protein in rice  

Kim, Ho-Bang (The Natural Science Research Institute, Myongji University)
Oh, Chang-Jae (School of Biological Sciences, College of Natural Sciences, Seoul National University)
Park, Yung-Chul (Department of Forest Environment Protection, College of Forest & Environmental Sciences, Kangwon National University)
Lee, Yi (Department of Industrial Plant Science & Technology, Chungbuk National University)
Choe, Sung-Hwa (School of Biological Sciences, College of Natural Sciences, Seoul National University)
An, Chung-Sun (School of Biological Sciences, College of Natural Sciences, Seoul National University)
Choi, Sang-Bong (Department of Biological Sciences, Myongji University)
Publication Information
BMB Reports / v.44, no.10, 2011 , pp. 680-685 More about this Journal
Abstract
The AT-hook motif is a small DNA-binding protein motif that has been found in the high mobility group of non-histone chromosomal proteins. The Arabidopsis genome contains 29 genes encoding the AT-hook motif DNA-binding protein (AHL). Recent studies of Arabidopsis genes (AtAHLs) have revealed that they might play diverse functional roles during plant growth and development. In this report, we mined 20 AHL genes (OsAHLs) from the rice genome database using AtAHL genes as queries and characterized their molecular features. A phylogenetic tree revealed that OsAHL proteins can be classified into 2 evolutionary clades. Tissue expression pattern analysis revealed that all of the OsAHL genes might be functionally expressed genes with 3 distinct expression patterns. Nuclear localization analysis using transgenic Arabidopsis showed that several OsAHL proteins are exclusively localized in the nucleus, indicating that they may act as architectural transcription factors to regulate expression of their target genes during plant growth and development.
Keywords
AT-hook motif DNA-binding protein; Light; Nuclear localization; Rice; Tissue expression;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
Times Cited By Web Of Science : 0  (Related Records In Web of Science)
Times Cited By SCOPUS : 0
연도 인용수 순위
1 Altschul, S. F., Gish, W., Miller, W., Meyers, E. W. and Lipman, D. (1990) Basic local alignment search tool. J. Mol. Biol. 215, 403-410.   DOI
2 Tamura, K., Dudley, J., Nei, M. and Kumar, S. (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24, 1596-1599.   DOI   ScienceOn
3 Clough, S. J. and Bent, A. F. (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-743.   DOI   ScienceOn
4 Meijer, A. H., van Dijk, E. L. and Hoge, J. H. (1996) Novel members of a family of AT hook-containing DNA-binding proteins from rice are identified through their in vitro interaction with consensus target sites of plant and animal homeodomain proteins. Plant Mol. Biol. 31, 607-618.   DOI
5 Gupta, R., Webster, C. I., Walker, A. and Gray, J. C. (1997) Chromosomal location and expression of the single-copy gene encoding high-mobility-group protein HMG-I/Y in Arabidopsis thaliana. Plant Mol. Biol. 34, 529-536.   DOI   ScienceOn
6 Gupta, R., Webster, C. I. and Gray, J. C. (1998) Characterization and promoter analysis of the Arabidopsis gene encoding high-mobility-group protein HMG-I/Y. Plant Mol. Biol. 36, 897-907.   DOI   ScienceOn
7 Zhao, J., Paul, L. K. and Grafi, G. (2009) The maize HMGA protein is localized to the nucleolus, can be acetylated in vitro at its globular domain and phosphorylation by CDK reduces its binding activity to AT-rich DNA. BBA - Gene Regulatory Mechanisms 1789, 751-757.
8 Zhao, J. and Grafi, G. (2000) The high mobility group I/Y protein is hypophosphorylated in endoreduplicating maize endosperm cells and is involved in alleviating histone H1-mediated transcriptional repression. J. Biol. Chem. 275, 27494-27499.
9 Yamamoto, S. and Minamikawa, T. (1997) The high mobility group protein HMG-Y binds to promoter regions of seed storage protein genes from Canavalia gladiata D.C. Plant Sci. 124, 165-173.   DOI   ScienceOn
10 Zhang, W., Wu, Q., Pwee, K. -H. and Kini, R. M. (2003) Interaction of wheat high-mobility-group proteins with four-way-junction DNA and characterization of the structure and expression of HMGA gene. Arch. Biochem. Biophys. 409, 357-366.   DOI   ScienceOn
11 Jung, K. -H., Jeon, J. -S. and An, G (2011) Web tools for rice transcriptome analyses. J. Plant Biol. 54, 65-80.   DOI   ScienceOn
12 Matsushita, A., Furumoto, T., Ishida, S. and Takahashi, Y. (2007) AGF1, an AT-hook protein, is necessary for the negative feedback of AtGA3ox1 encoding GA 3-oxidase. Plant Physiol. 143, 1152-1162.   DOI   ScienceOn
13 Vom Endt, D., Soares e Silva, M., Kijne, J. W., Pasquali, G. and Memelink, J. (2007) Identification of a bipartite jasmonate-responsive promoter element in the Catharanthus roseus ORCA3 transcription factor gene that interacts specifically with AT-Hook DNA-binding proteins. Plant Physiol. 144, 1680-1689.   DOI   ScienceOn
14 Lim, P. O., Kim, Y., Breeze, E., Koo, J. C., Woo, H. R., Ryu, J. S., Park, D. H., Beynon, J., Tabrett, A., Buchanan- Wollsston, V. and Nam, H. G. (2007) Overexpression of a chromatin architecture-controlling AT-hook protein extends leaf longevity and increases the post-harvest storage life of plants. Plant J. 52, 1140-1153.   DOI   ScienceOn
15 Nieto-Sotelo, J., Ichida, A. and Quail, P. H. (1994) PF1: an A-T hook-containing DNA binding protein from rice that interacts with a functionally defined d(AT)-rich element in the oat phytochrome A3 gene promoter. Plant Cell 6, 287-301.   DOI   ScienceOn
16 Street, I. H., Shah, P. K., Smith, A. M., Avery, N. and Neff, M. M. (2008) The AT-hook-containing proteins SOB3/AHL29 and ESC/AHL27 are negative modulators of hypocotyl growth in Arabidopsis. Plant J. 54, 1-14.
17 Xiao, C., Chen, F., Yu, X., Lin, C. and Fu, Y. -F. (2009) Over-expression of an AT-hook gene, AHL22, delays flowering and inhibits the elongation of the hypocotyl in Arabidopsis thaliana. Plant Mol. Biol. 71, 39-50.   DOI
18 Ng, K.-H., Yu, H. and Ito, T (2009) AGAMOUS controls GIANT KILLER, a multifunctional chromatin modifier in reproductive organ patterning and differentiation. PLoS Biol. 7(11), e1000251. doi:10,1371/journal.pbio.1000251.   DOI
19 Sikder, D. and Kodadek, T. (2005) Genomic studies of transcription factor-DNA interactions. Curr. Opin. Chem. Biol. 9, 38-45.   DOI   ScienceOn
20 Zhao, K., Kas, E., Gonzales, E. and Laemmli, U. K. (1993) SAR-dependent mobilization of histone H1 by HMG-I/Y in vitro: HMG-I/Y is enriched in H1-depleted chromatin. EMBO J. 12, 3237-3247.
21 Rajeswari, M. R. and Jain, A. (2002) High-mobility-group chromosomal proteins, HMGA1 as potential tumour markers. Current Sci. 82, 838-844.
22 Grasser, K. D. (2003) Chromatin-associated HMGA and HMGB proteins: versatile co-regulators of DNA-dependent processes. Plant Mol. Biol. 53, 281-295.   DOI   ScienceOn
23 Morisawa, G., Han-Yama, A., Moda, I., Tamai, A., Iwabuchi, M. and Meshi, T. (2000) AHM1, a novel type of nuclear matrix-localized, MAR binding protein with a single AT hook and a J domain-homologous region. Plant Cell 12, 1903-1916.   DOI
24 Aravind, L. and Landsman, D. (1998) AT-hook motifs identified in a wide variety of DNA-binding proteins. Nucleic Acids Res. 26, 4413-4421.   DOI   ScienceOn
25 Reeves, R. and Beckerbauer, L. (2001) HMGI/Y proteins: flexible regulators of transcription and chromatin structure. Biochim. Biophys. Acta. 1519, 13-29.   DOI   ScienceOn
26 Strick, R. and Laemmli, U. K. (1995) SARs are cis DNA elements of chromosome dynamics: synthesis of a SAR repressor protein. Cell 83, 1137-1148.   DOI   ScienceOn
27 Fujimoto, S., Matsunaga, S., Yonemura, M., Uchiyama, S., Azuma, T. and Fukui, K. (2004) Identification of a novel plant MAR DNA binding protein localized on chromosomal surfaces. Plant Mol. Biol. 56, 225-239.   DOI