Repression of tyrosine hydroxylase is responsible for the sex-linked chocolate mutation of the silkworm, Bombyx mori

Chun Liu, Kimiko Yamamoto, Ting Cai Cheng, Keiko Kadono-Okuda, Junko Narukawa, Shi Ping Liu, Yu Han, Ryo Futahashi, Kurako Kidokoro, Hiroaki Noda, Isao Kobayashi, Toshiki Tamura, Akio Ohnuma, Yutaka Banno, Fang Ying Dai, Zhong Huai Xiang, Marian R. Goldsmith, Kazuei Mita, Qing You Xia

研究成果: ジャーナルへの寄稿記事

57 引用 (Scopus)

抄録

Pigmentation patterning has long interested biologists, integrating topics in ecology, development, genetics, and physiology. Wild-type neonatal larvae of the silkworm, Bombyx mori, are completely black. By contrast, the epidermis and head of larvae of the homozygous recessive sex-linked chocolate (sch) mutant are reddish brown. When incubated at 30 °C, mutants with the sch allele fail to hatch; moreover, homozygous mutants carrying the allele sch lethal (sch l) do not hatch even at room temperature (25 °C). By positional cloning, we narrowed a region containing sch to 239,622 bp on chromosome 1 using 4,501 backcross (BC1) individuals. Based on expression analyses, the best sch candidate gene was shown to be tyrosine hydroxylase (BmTh). BmTh coding sequences were identical among sch, schl, and wild-type. However, in sch the ∼70-kb sequence was replaced with ∼4.6 kb of a Tc1-mariner type transposon located ∼6 kb upstream of BmTh, and in schl, a large fragment of an L1Bm retrotransposon was inserted just in front of the transcription start site of BmTh. In both cases, we observed a drastic reduction of BmTh expression. Use of RNAi with BmTh prevented pigmentation and hatching, and feeding of a tyrosine hydroxylase inhibitor also suppressed larval pigmentation in the wild-type strain, pnd+ and in a pS (black-striped) heterozygote. Feeding L-dopa to sch neonate larvae rescued the mutant phenotype from chocolate to black. Our results indicate the BmTh gene is responsible for the sch mutation, which plays an important role in melanin synthesis producing neonatal larval color.

元の言語英語
ページ(範囲)12980-12985
ページ数6
ジャーナルProceedings of the National Academy of Sciences of the United States of America
107
発行部数29
DOI
出版物ステータス出版済み - 7 20 2010

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Safe Sex
Bombyx
Tyrosine 3-Monooxygenase
Mutation
Pigmentation
Larva
Chocolate
Alleles
Retroelements
Chromosomes, Human, Pair 1
Transcription Initiation Site
Melanins
Levodopa
Heterozygote
RNA Interference
Ecology
Epidermis
Genes
Organism Cloning
Color

All Science Journal Classification (ASJC) codes

  • General

これを引用

Repression of tyrosine hydroxylase is responsible for the sex-linked chocolate mutation of the silkworm, Bombyx mori. / Liu, Chun; Yamamoto, Kimiko; Cheng, Ting Cai; Kadono-Okuda, Keiko; Narukawa, Junko; Liu, Shi Ping; Han, Yu; Futahashi, Ryo; Kidokoro, Kurako; Noda, Hiroaki; Kobayashi, Isao; Tamura, Toshiki; Ohnuma, Akio; Banno, Yutaka; Dai, Fang Ying; Xiang, Zhong Huai; Goldsmith, Marian R.; Mita, Kazuei; Xia, Qing You.

:: Proceedings of the National Academy of Sciences of the United States of America, 巻 107, 番号 29, 20.07.2010, p. 12980-12985.

研究成果: ジャーナルへの寄稿記事

Liu, C, Yamamoto, K, Cheng, TC, Kadono-Okuda, K, Narukawa, J, Liu, SP, Han, Y, Futahashi, R, Kidokoro, K, Noda, H, Kobayashi, I, Tamura, T, Ohnuma, A, Banno, Y, Dai, FY, Xiang, ZH, Goldsmith, MR, Mita, K & Xia, QY 2010, 'Repression of tyrosine hydroxylase is responsible for the sex-linked chocolate mutation of the silkworm, Bombyx mori', Proceedings of the National Academy of Sciences of the United States of America, 巻. 107, 番号 29, pp. 12980-12985. https://doi.org/10.1073/pnas.1001725107
Liu, Chun ; Yamamoto, Kimiko ; Cheng, Ting Cai ; Kadono-Okuda, Keiko ; Narukawa, Junko ; Liu, Shi Ping ; Han, Yu ; Futahashi, Ryo ; Kidokoro, Kurako ; Noda, Hiroaki ; Kobayashi, Isao ; Tamura, Toshiki ; Ohnuma, Akio ; Banno, Yutaka ; Dai, Fang Ying ; Xiang, Zhong Huai ; Goldsmith, Marian R. ; Mita, Kazuei ; Xia, Qing You. / Repression of tyrosine hydroxylase is responsible for the sex-linked chocolate mutation of the silkworm, Bombyx mori. :: Proceedings of the National Academy of Sciences of the United States of America. 2010 ; 巻 107, 番号 29. pp. 12980-12985.
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abstract = "Pigmentation patterning has long interested biologists, integrating topics in ecology, development, genetics, and physiology. Wild-type neonatal larvae of the silkworm, Bombyx mori, are completely black. By contrast, the epidermis and head of larvae of the homozygous recessive sex-linked chocolate (sch) mutant are reddish brown. When incubated at 30 °C, mutants with the sch allele fail to hatch; moreover, homozygous mutants carrying the allele sch lethal (sch l) do not hatch even at room temperature (25 °C). By positional cloning, we narrowed a region containing sch to 239,622 bp on chromosome 1 using 4,501 backcross (BC1) individuals. Based on expression analyses, the best sch candidate gene was shown to be tyrosine hydroxylase (BmTh). BmTh coding sequences were identical among sch, schl, and wild-type. However, in sch the ∼70-kb sequence was replaced with ∼4.6 kb of a Tc1-mariner type transposon located ∼6 kb upstream of BmTh, and in schl, a large fragment of an L1Bm retrotransposon was inserted just in front of the transcription start site of BmTh. In both cases, we observed a drastic reduction of BmTh expression. Use of RNAi with BmTh prevented pigmentation and hatching, and feeding of a tyrosine hydroxylase inhibitor also suppressed larval pigmentation in the wild-type strain, pnd+ and in a pS (black-striped) heterozygote. Feeding L-dopa to sch neonate larvae rescued the mutant phenotype from chocolate to black. Our results indicate the BmTh gene is responsible for the sch mutation, which plays an important role in melanin synthesis producing neonatal larval color.",
author = "Chun Liu and Kimiko Yamamoto and Cheng, {Ting Cai} and Keiko Kadono-Okuda and Junko Narukawa and Liu, {Shi Ping} and Yu Han and Ryo Futahashi and Kurako Kidokoro and Hiroaki Noda and Isao Kobayashi and Toshiki Tamura and Akio Ohnuma and Yutaka Banno and Dai, {Fang Ying} and Xiang, {Zhong Huai} and Goldsmith, {Marian R.} and Kazuei Mita and Xia, {Qing You}",
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T1 - Repression of tyrosine hydroxylase is responsible for the sex-linked chocolate mutation of the silkworm, Bombyx mori

AU - Liu, Chun

AU - Yamamoto, Kimiko

AU - Cheng, Ting Cai

AU - Kadono-Okuda, Keiko

AU - Narukawa, Junko

AU - Liu, Shi Ping

AU - Han, Yu

AU - Futahashi, Ryo

AU - Kidokoro, Kurako

AU - Noda, Hiroaki

AU - Kobayashi, Isao

AU - Tamura, Toshiki

AU - Ohnuma, Akio

AU - Banno, Yutaka

AU - Dai, Fang Ying

AU - Xiang, Zhong Huai

AU - Goldsmith, Marian R.

AU - Mita, Kazuei

AU - Xia, Qing You

PY - 2010/7/20

Y1 - 2010/7/20

N2 - Pigmentation patterning has long interested biologists, integrating topics in ecology, development, genetics, and physiology. Wild-type neonatal larvae of the silkworm, Bombyx mori, are completely black. By contrast, the epidermis and head of larvae of the homozygous recessive sex-linked chocolate (sch) mutant are reddish brown. When incubated at 30 °C, mutants with the sch allele fail to hatch; moreover, homozygous mutants carrying the allele sch lethal (sch l) do not hatch even at room temperature (25 °C). By positional cloning, we narrowed a region containing sch to 239,622 bp on chromosome 1 using 4,501 backcross (BC1) individuals. Based on expression analyses, the best sch candidate gene was shown to be tyrosine hydroxylase (BmTh). BmTh coding sequences were identical among sch, schl, and wild-type. However, in sch the ∼70-kb sequence was replaced with ∼4.6 kb of a Tc1-mariner type transposon located ∼6 kb upstream of BmTh, and in schl, a large fragment of an L1Bm retrotransposon was inserted just in front of the transcription start site of BmTh. In both cases, we observed a drastic reduction of BmTh expression. Use of RNAi with BmTh prevented pigmentation and hatching, and feeding of a tyrosine hydroxylase inhibitor also suppressed larval pigmentation in the wild-type strain, pnd+ and in a pS (black-striped) heterozygote. Feeding L-dopa to sch neonate larvae rescued the mutant phenotype from chocolate to black. Our results indicate the BmTh gene is responsible for the sch mutation, which plays an important role in melanin synthesis producing neonatal larval color.

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