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The first 100% eukaryotic genome sequences from the red alga Cyanidioschyzon merolae 10D

The biological sciences have been embracing a new paradigm as a result of accruing genome information. However, all previously reported eukaryotic nuclear genome sequences have been incomplete, especially in highly repeated units and chromosomal ends. Because repetitive DNA is essential to genome fu...

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Bibliographic Details
Published in:Journal of plant research 2006-12, Vol.119, p.181-181
Main Authors: Nozaki, H, Takano, H, Misumi, O, Terasawa, K, Matuzaki, M, Maruyama, S, Takio, S, Tamura, K, Chung, S J, Nakamura, S, Kuroiwa, H, Tanaka, K, Sato, N, Kuroiwa, T
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Language:English
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Summary:The biological sciences have been embracing a new paradigm as a result of accruing genome information. However, all previously reported eukaryotic nuclear genome sequences have been incomplete, especially in highly repeated units and chromosomal ends. Because repetitive DNA is essential to genome function, and may contribute to the diversity of isoforms and the evolution of life, complete chromosomal structures are fundamental for understanding eukaryotic cells. Here we show the first 100% complete nuclear genome sequence, based on completely filling contig gaps and end-sequencing of chromosomal ends, in the hot spring red alga Cyanidioschyzon merolae 10D (Matsuzaki et al. 2004, Nature). All histone genes are localised in a single chromosome, representing the smallest histone cluster area known in eukaryotes. The basic telomere repeat sequence (AATGGGGGG), which was confirmed for all chromosomal ends, suggests two possible telomere RNA subunit genes. Although transposable elements are extremely infrequent, novel repetitive elements cover approximately 5% of the whole sequence. The 100% eukaryotic genome sequence reported here, along with the previously reported complete mitochondrial and plastid genomes, should greatly improve the precision of various biological analyses and serve as a firm foundation for future biological research, especially proteomics and structural biology with heat-stable proteins.
ISSN:0918-9440