The Conserved Proline Residue in the LOB Domain of LBD18 Is Critical for DNA-Binding and Biological Function

• Published in: Molecular plant 2013-09, Vol.6 (5), p.1722-1725
• Main Authors: Lee, Han Woo, Kim, Min-Jung, Park, Moung Yeon, Han, Kyung-Hwan, Kim, Jungmook
• Format: Article
• Language: English
• Subjects: Amino Acid Motifs; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis Proteins - chemistry; Arabidopsis Proteins - metabolism; Conserved Sequence; DNA, Plant - metabolism; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - metabolism; DNA结合; LOB; Plants, Genetically Modified; Proline - metabolism; Protein Structure, Tertiary; Structure-Activity Relationship; Transcription Factors - chemistry; Transcription Factors - metabolism; Transgenes - genetics; 亮氨酸拉链; 保守; 器官发育; 残基; 生物学功能; 脯氨酸
• ISSN: 1674-2052; 1752-9867
• DOI: 10.1093/mp/sst037

Dear Editor, The LATERAL ORGAN BOUNDARIES DOMAIN （LBD）/ ASYMMETRICLEAVES2-LIKE （ASL） genes （hereafter referred to as LBD） encode proteins containing a conserved plant-specific LOB domain and play roles in lateral organ development （Iwakawa et al., 2002; Shuai et al., 2002; Majer and Hochholdinger, 2011）. The LOB domain is approximately 100 amino acids in length and contains a conserved four-Cys motif （CX2CX6CX3C）, the Gly-Ala-Ser block （GAS）, and the leucine-zipper-like coiled-coil motif （LX6LX3LX6L） （Shuai et al., 2002）. The leucine-zipper-like coiled-coil motif in the LOB domain is predicted to function in protein dimerization. LOB, AS2, and LBD4 preferentially bind unique DNA sequences in electrophoretic mobility shift assays （EMSAs） （Husbands et al., 2007）. The LOB domain of AS2 cannot be functionally replaced by those of other members of the LOB family,