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Prdm9 polymorphism unveils mouse evolutionary tracks.

Kono H, Tamura M, Osada N, Suzuki H, Abe K, Moriwaki K, Ohta K, Shiroishi T - DNA Res. (2014)

Bottom Line: Nevertheless, information about Prdm9 sequences in natural populations is very limited.Prdm9 alleles specific to various M. musculus subspecies dominate in subspecies territories.Moreover, introgression into other subspecies territories was found for highly divergent Prdm9 alleles associated with t-haplotype.

View Article: PubMed Central - PubMed

Affiliation: Mammalian Genetics Laboratory, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan Department of Biophysics and Biochemistry, The University of Tokyo, Tokyo 153-8902, Japan.

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Amino acid variation in Prdm9 ZF repeats. (A) Multiple alignment of ZF repeat sequences from inbred strains and wild-captured mice. The alignments were made separately for the first repeat, the internal repeats of the ZFA, and the last repeat, as their degrees of variation are different (see text). The α-helix domain of the ZF is shown at top of the internal repeat. The one-letter code is shown to the left of the repeats. A novel repeat found in this study is indicated by # to the right of the repeat. Amino acid variation at specific positions along aligned ZF repeats are shown in colour. The star on the left side in the first repeat corresponds to those shown in Fig. 3. (B) Multiple alignment of ZF repeats of human PRDM9 based on the publically available data (http://www.ncbi.nlm.nih.gov/nuccore). The format of the alignment is the same as that used for mouse Prdm9.
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DST059F2: Amino acid variation in Prdm9 ZF repeats. (A) Multiple alignment of ZF repeat sequences from inbred strains and wild-captured mice. The alignments were made separately for the first repeat, the internal repeats of the ZFA, and the last repeat, as their degrees of variation are different (see text). The α-helix domain of the ZF is shown at top of the internal repeat. The one-letter code is shown to the left of the repeats. A novel repeat found in this study is indicated by # to the right of the repeat. Amino acid variation at specific positions along aligned ZF repeats are shown in colour. The star on the left side in the first repeat corresponds to those shown in Fig. 3. (B) Multiple alignment of ZF repeats of human PRDM9 based on the publically available data (http://www.ncbi.nlm.nih.gov/nuccore). The format of the alignment is the same as that used for mouse Prdm9.

Mentions: We aligned all ZF repeats identified in this study (Fig. 2A). The first ZF repeat appears to be uniform, but the internal ZF repeats were highly variable. In particular, DNA recognition positions −1, 3, and 6 were highly variable (Fig. 2A), consistent with a previous report.17 A lower level of variation was found at positions, −5, −2, and 1. The last repeat tends to be less variable than the internal repeats. In total, we identified 36 unique ZF repeats in ZFA. Of these, 24 are newly identified in this study (Fig. 2A).Figure 2.


Prdm9 polymorphism unveils mouse evolutionary tracks.

Kono H, Tamura M, Osada N, Suzuki H, Abe K, Moriwaki K, Ohta K, Shiroishi T - DNA Res. (2014)

Amino acid variation in Prdm9 ZF repeats. (A) Multiple alignment of ZF repeat sequences from inbred strains and wild-captured mice. The alignments were made separately for the first repeat, the internal repeats of the ZFA, and the last repeat, as their degrees of variation are different (see text). The α-helix domain of the ZF is shown at top of the internal repeat. The one-letter code is shown to the left of the repeats. A novel repeat found in this study is indicated by # to the right of the repeat. Amino acid variation at specific positions along aligned ZF repeats are shown in colour. The star on the left side in the first repeat corresponds to those shown in Fig. 3. (B) Multiple alignment of ZF repeats of human PRDM9 based on the publically available data (http://www.ncbi.nlm.nih.gov/nuccore). The format of the alignment is the same as that used for mouse Prdm9.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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Show All Figures
getmorefigures.php?uid=PMC4060951&req=5

DST059F2: Amino acid variation in Prdm9 ZF repeats. (A) Multiple alignment of ZF repeat sequences from inbred strains and wild-captured mice. The alignments were made separately for the first repeat, the internal repeats of the ZFA, and the last repeat, as their degrees of variation are different (see text). The α-helix domain of the ZF is shown at top of the internal repeat. The one-letter code is shown to the left of the repeats. A novel repeat found in this study is indicated by # to the right of the repeat. Amino acid variation at specific positions along aligned ZF repeats are shown in colour. The star on the left side in the first repeat corresponds to those shown in Fig. 3. (B) Multiple alignment of ZF repeats of human PRDM9 based on the publically available data (http://www.ncbi.nlm.nih.gov/nuccore). The format of the alignment is the same as that used for mouse Prdm9.
Mentions: We aligned all ZF repeats identified in this study (Fig. 2A). The first ZF repeat appears to be uniform, but the internal ZF repeats were highly variable. In particular, DNA recognition positions −1, 3, and 6 were highly variable (Fig. 2A), consistent with a previous report.17 A lower level of variation was found at positions, −5, −2, and 1. The last repeat tends to be less variable than the internal repeats. In total, we identified 36 unique ZF repeats in ZFA. Of these, 24 are newly identified in this study (Fig. 2A).Figure 2.

Bottom Line: Nevertheless, information about Prdm9 sequences in natural populations is very limited.Prdm9 alleles specific to various M. musculus subspecies dominate in subspecies territories.Moreover, introgression into other subspecies territories was found for highly divergent Prdm9 alleles associated with t-haplotype.

View Article: PubMed Central - PubMed

Affiliation: Mammalian Genetics Laboratory, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan Department of Biophysics and Biochemistry, The University of Tokyo, Tokyo 153-8902, Japan.

Show MeSH
Related in: MedlinePlus