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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.

Matsumura Y, Iwakawa H, Machida Y, Machida C - Plant J. (2009)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Plant Biology Research Center, Chubu University, 1200 Matsumoto-cho, Kasugai, Aichi 487-8501, Japan.

ABSTRACT
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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Comparison of the predicted amino acid sequences of the C-terminal halves of products of genes in the AS2/LOB family. Each number indicates the identity, as a percentage, between the predicted amino acid sequences of indicated proteins, as determined with the Maximum Matching program of GENETYX-MAC ver. 13. Percentages greater than 35% are shaded. Numbers in percentages under group designations indicate the identities between entire amino acid sequences.
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fig02: Comparison of the predicted amino acid sequences of the C-terminal halves of products of genes in the AS2/LOB family. Each number indicates the identity, as a percentage, between the predicted amino acid sequences of indicated proteins, as determined with the Maximum Matching program of GENETYX-MAC ver. 13. Percentages greater than 35% are shaded. Numbers in percentages under group designations indicate the identities between entire amino acid sequences.

Mentions: We compared the deduced amino acid sequences of the C-terminal halves (the regions downstream of the respective AS2/LOB domains) of all members of the gene family (Figure 2). No deduced product of any ASL/LBD gene exhibited any significant similarity, in terms of amino acid sequence, to the C-terminal half of AS2.


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.

Matsumura Y, Iwakawa H, Machida Y, Machida C - Plant J. (2009)

Comparison of the predicted amino acid sequences of the C-terminal halves of products of genes in the AS2/LOB family. Each number indicates the identity, as a percentage, between the predicted amino acid sequences of indicated proteins, as determined with the Maximum Matching program of GENETYX-MAC ver. 13. Percentages greater than 35% are shaded. Numbers in percentages under group designations indicate the identities between entire amino acid sequences.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2721968&req=5

fig02: Comparison of the predicted amino acid sequences of the C-terminal halves of products of genes in the AS2/LOB family. Each number indicates the identity, as a percentage, between the predicted amino acid sequences of indicated proteins, as determined with the Maximum Matching program of GENETYX-MAC ver. 13. Percentages greater than 35% are shaded. Numbers in percentages under group designations indicate the identities between entire amino acid sequences.
Mentions: We compared the deduced amino acid sequences of the C-terminal halves (the regions downstream of the respective AS2/LOB domains) of all members of the gene family (Figure 2). No deduced product of any ASL/LBD gene exhibited any significant similarity, in terms of amino acid sequence, to the C-terminal half of AS2.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Plant Biology Research Center, Chubu University, 1200 Matsumoto-cho, Kasugai, Aichi 487-8501, Japan.

ABSTRACT
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.

Show MeSH