4.8 Article

Characterization of genes in the ASYMMETRIC LEAVES2/LATERAL ORGAN BOUNDARIES (AS2/LOB) family in Arabidopsis thaliana, and functional and molecular comparisons between AS2 and other family members

期刊

PLANT JOURNAL
卷 58, 期 3, 页码 525-537

出版社

WILEY
DOI: 10.1111/j.1365-313X.2009.03797.x

关键词

ASYMMETRIC LEAVES2 (AS2); AS2-like; LOB domain (ASL; LBD) gene; AS2; LOB family; AS2; LOB domain; plant development

资金

  1. Japan Science and Technology Corporation [1403621, 19060036, 16027250, 15570181]
  2. Ministry of Education, Science, Culture, Sports and Technology, Japan
  3. Global Center of Excellence Program for the Division of Biological Science, Nagoya University
  4. Grants-in-Aid for Scientific Research [16027250, 21570052, 15570181] Funding Source: KAKEN

向作者/读者索取更多资源

The ASYMMETRIC LEAVES2 (AS2) gene is required for the generation of the flat and symmetrical shape of the leaf lamina in Arabidopsis. AS2 encodes a plant-specific protein with an AS2/LATERAL ORGAN BOUNDARIES (AS2/LOB) domain that includes a cysteine repeat, a conserved single glycine residue and a leucine-zipper-like sequence in its amino-terminal half. The Arabidopsis genome contains 42 genes, including AS2, that encode proteins with an AS2/LOB domain in their amino-terminal halves, and these genes constitute the AS2/LOB gene family. In the present study, we cloned and characterized cDNAs that covered the putative coding regions of all members of this family, and investigated patterns of transcription systematically in Arabidopsis plants. Comparisons among amino acid sequences that had been deduced from the cloned cDNAs revealed eight groups of genes, with two or three members each, and high degrees of identity among entire amino acid sequences, suggesting that some members of the AS2/LOB family might have redundant function(s). Moreover, no member of the family exhibited significant similarity, in terms of the deduced amino acid sequence of the carboxy-terminal half, to AS2. Results of domain swapping between AS2 and other members of the family showed that the AS2/LOB domain of AS2 cannot be functionally replaced by those of other members of the family, and that only a few dissimilarities among respective amino acid residues of the AS2/LOB domain of AS2 and those of other members are important for the specific functions of AS2.

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