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Chloroplast-encoded serotonin N-acetyltransferase in the red alga Pyropia yezoensis: gene transition to the nucleus from chloroplasts.

Byeon Y, Yool Lee H, Choi DW, Back K - J. Exp. Bot. (2014)

Bottom Line: Melatonin was present at 0.16ng g(-1) of fresh mass but increased during heat stress.Phylogenetic analysis of the sequence suggested that PySNAT has evolved from the cyanobacteria SNAT gene via endosymbiotic gene transfer.Additionally, the chloroplast transit peptides of plant SNATs were acquired 1500 million years ago, concurrent with the appearance of green algae.

View Article: PubMed Central - PubMed

Affiliation: Department of Biotechnology, Interdisciplinary Program of Bioenergy and Biomaterials, Bioenergy Research Center, College of Agriculture and Life Sciences, Chonnam National University, Gwangju, Republic of Korea.

No MeSH data available.


Related in: MedlinePlus

(A) Comparison of the deduced amino acid sequences of SNAT from rice (GenBank accession no. AK059369), cyanobacteria (NP_442603), and laver (NC_007932). The conserved acetyl-CoA binding motif is underlined. The asterisks denote identity. Dashes indicate gaps that were introduced to maximize homology. Amino acid residues predicted to be chloroplast transit sequences are boxed. (B) Phylogenetic analysis of SNAT homologues from rice, loblolly pine, cyanobacteria, and laver. Numbers denote branch support values of each node. Bar, 0.3 substitutions per site.
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Figure 1: (A) Comparison of the deduced amino acid sequences of SNAT from rice (GenBank accession no. AK059369), cyanobacteria (NP_442603), and laver (NC_007932). The conserved acetyl-CoA binding motif is underlined. The asterisks denote identity. Dashes indicate gaps that were introduced to maximize homology. Amino acid residues predicted to be chloroplast transit sequences are boxed. (B) Phylogenetic analysis of SNAT homologues from rice, loblolly pine, cyanobacteria, and laver. Numbers denote branch support values of each node. Bar, 0.3 substitutions per site.

Mentions: The rice SNAT gene exists as a single copy in the rice genome and is highly conserved in plant lineages, including cyanobacteria (Byeon et al., 2013). According to BLAST analysis, plant SNAT homologues have been found in the nuclear genome in all members of Chlorophyta that were examined, such as green algae and terrestrial plants, but the SNAT homologue was located in chloroplasts in rhodophyta, including red algae such as laver (Pyropia yezoensis). Therefore, we explored whether the chloroplast-encoded SNAT in red algae showed SNAT enzyme activity. We cloned the chloroplast-encoded SNAT homologue from Pyropia yezoensis (PySNAT). PySNAT was 174 aa with a calculated molecular weight of approximately 20099Da (Fig. 1). The PySNAT polypeptides shared 50% identity with the cyanobacteria SNAT and also showed high identity to rice and loblolly pine at 45 and 43%, respectively, when compared with the level of mature polypeptides of rice and loblolly pine. The theoretical isoelectric point (pI) was higher in PySNAT (9.36) than cyanobacteria SNAT (pI 7.78), but G+C content decreased to 29% in PySNAT relative to 51% in cyanobacteria SNAT. Phylogenetic analysis revealed that PySNAT is placed in the same clade as the cyanobacteria SNAT, suggesting that PySNAT originated from cyanobacteria via endosymbiosis. Unlike loblolly pine and rice SNAT polypeptides, no N-terminal extension peptides were observed as a chloroplast transit peptide.


Chloroplast-encoded serotonin N-acetyltransferase in the red alga Pyropia yezoensis: gene transition to the nucleus from chloroplasts.

Byeon Y, Yool Lee H, Choi DW, Back K - J. Exp. Bot. (2014)

(A) Comparison of the deduced amino acid sequences of SNAT from rice (GenBank accession no. AK059369), cyanobacteria (NP_442603), and laver (NC_007932). The conserved acetyl-CoA binding motif is underlined. The asterisks denote identity. Dashes indicate gaps that were introduced to maximize homology. Amino acid residues predicted to be chloroplast transit sequences are boxed. (B) Phylogenetic analysis of SNAT homologues from rice, loblolly pine, cyanobacteria, and laver. Numbers denote branch support values of each node. Bar, 0.3 substitutions per site.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4321536&req=5

Figure 1: (A) Comparison of the deduced amino acid sequences of SNAT from rice (GenBank accession no. AK059369), cyanobacteria (NP_442603), and laver (NC_007932). The conserved acetyl-CoA binding motif is underlined. The asterisks denote identity. Dashes indicate gaps that were introduced to maximize homology. Amino acid residues predicted to be chloroplast transit sequences are boxed. (B) Phylogenetic analysis of SNAT homologues from rice, loblolly pine, cyanobacteria, and laver. Numbers denote branch support values of each node. Bar, 0.3 substitutions per site.
Mentions: The rice SNAT gene exists as a single copy in the rice genome and is highly conserved in plant lineages, including cyanobacteria (Byeon et al., 2013). According to BLAST analysis, plant SNAT homologues have been found in the nuclear genome in all members of Chlorophyta that were examined, such as green algae and terrestrial plants, but the SNAT homologue was located in chloroplasts in rhodophyta, including red algae such as laver (Pyropia yezoensis). Therefore, we explored whether the chloroplast-encoded SNAT in red algae showed SNAT enzyme activity. We cloned the chloroplast-encoded SNAT homologue from Pyropia yezoensis (PySNAT). PySNAT was 174 aa with a calculated molecular weight of approximately 20099Da (Fig. 1). The PySNAT polypeptides shared 50% identity with the cyanobacteria SNAT and also showed high identity to rice and loblolly pine at 45 and 43%, respectively, when compared with the level of mature polypeptides of rice and loblolly pine. The theoretical isoelectric point (pI) was higher in PySNAT (9.36) than cyanobacteria SNAT (pI 7.78), but G+C content decreased to 29% in PySNAT relative to 51% in cyanobacteria SNAT. Phylogenetic analysis revealed that PySNAT is placed in the same clade as the cyanobacteria SNAT, suggesting that PySNAT originated from cyanobacteria via endosymbiosis. Unlike loblolly pine and rice SNAT polypeptides, no N-terminal extension peptides were observed as a chloroplast transit peptide.

Bottom Line: Melatonin was present at 0.16ng g(-1) of fresh mass but increased during heat stress.Phylogenetic analysis of the sequence suggested that PySNAT has evolved from the cyanobacteria SNAT gene via endosymbiotic gene transfer.Additionally, the chloroplast transit peptides of plant SNATs were acquired 1500 million years ago, concurrent with the appearance of green algae.

View Article: PubMed Central - PubMed

Affiliation: Department of Biotechnology, Interdisciplinary Program of Bioenergy and Biomaterials, Bioenergy Research Center, College of Agriculture and Life Sciences, Chonnam National University, Gwangju, Republic of Korea.

No MeSH data available.


Related in: MedlinePlus