コヒーシン
染色体を分配結合させる機能を持つタンパク質。「染色体接着因子」とも呼ばれる。卵母細胞が分化(減数分裂)して卵子を生じる際には染色体を正しく配分する役割を担う。
理化学研究所は2015年7月1日に、加齢の進んだマウスの卵母細胞の染色体数を観察して加齢に伴う卵子の染色体数異常の主要因を明らかにしたと発表した。加齢とともにコヒーシンが染色体上から減少し、これによって卵母細胞が減数分裂する際に染色体分配にエラーが生じやすくなる、という仮説の裏付けとなる減少が、実験により観察されたという。
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加齢による卵子の染色体数異常の原因を特定-染色体分配の誤りを直接観察することにより解明- - 理化学研究所 プレスリリース(研究成果)2015年7月1日
コヒーシン
酵素タンパク質モチーフなど: | グロブリン ケラチン ゲルゾリン コヒーシン コラゲナーゼ コラーゲン コラーゲンヘリックス |
コヒーシン
出典: フリー百科事典『ウィキペディア(Wikipedia)』 (2023/11/08 13:31 UTC 版)
コヒーシン(こひーしん:cohesin)は、姉妹染色分体の接着(複製された染色体を娘細胞に均等に分離するために必須な過程; sister chromatid cohesion)に中心的な役割を果たすタンパク質複合体である[1][2] 。
- ^ Nasmyth K, Haering CH (2009). “Cohesin: its roles and mechanisms”. Annu. Rev. Genet. 43: 525-558. PMID 19886810.
- ^ Onn I, Heidinger-Pauli JM, Guacci V, Unal E, Koshland DE (2008). “Sister chromatid cohesion: a simple concept with a complex reality”. Annu. Rev. Cell Dev. Biol. 24: 105-129. PMID 18616427.
- ^ Jeppsson K, Kanno T, Shirahige K, Sjögren C (2014). “The maintenance of chromosome structure: positioning and functioning of SMC complexes”. Nat. Rev. Mol. Cell Biol. 15: 601-614. PMID 25145851.
- ^ Uhlmann F (2016). “SMC complexes: from DNA to chromosomes”. Nat. Rev. Mol. Cell Biol. 17: 399-412. PMID 27075410.
- ^ Schleiffer A, Kaitna S, Maurer-Stroh S, Glotzer M, Nasmyth K, Eisenhaber F (2003). “Kleisins: a superfamily of bacterial and eukaryotic SMC protein partners”. Mol. Cell 11 (3): 571-575. PMID 12667442.
- ^ Neuwald AF, Hirano T (2000). “HEAT repeats associated with condensins, cohesins, and other complexes involved in chromosome-related functions”. Genome Res. 10 (10): 1445-52. PMID 11042144.
- ^ Yoshimura SH, Hirano T (2016). “HEAT repeats - versatile arrays of amphiphilic helices working in crowded environments?”. J. Cell Sci. 129 (21): 3963-3970. PMID 27802131.
- ^ Michaelis C, Ciosk R, Nasmyth K (1997). “Cohesins: chromosomal proteins that prevent premature separation of sister chromatids”. Cell 91 (1): 35-45. PMID 9335333.
- ^ Guacci V, Koshland D, Strunnikov A (1997). “A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae”. Cell 91 (1): 47-57. PMID 9335334.
- ^ a b c Tóth A, Ciosk R, Uhlmann F, Galova M, Schleiffer A, Nasmyth K (1999). “Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication”. Genes Dev 13 (3): 320-333. PMID 9990856.
- ^ Losada A, Hirano M, Hirano T (1998). “Identification of Xenopus SMC protein complexes required for sister chromatid cohesion”. Genes Dev. 12 (13): 1986-1997. PMID 9649503.
- ^ Losada A, Yokochi T, Kobayashi R, Hirano T (2000). “Identification and characterization of SA/Scc3p subunits in the Xenopus and human cohesin complexes”. J. Cell Biol. 150 (3): 405-416. PMID 10931856.
- ^ Watanabe Y, Nurse P (1999). “Cohesin Rec8 is required for reductional chromosome segregation at meiosis”. Nature 400: 461-464. PMID 10440376.
- ^ Revenkova E, Eijpe M, Heyting C, Gross B, Jessberger R (2001). “Novel meiosis-specific isoform of mammalian SMC1”. Mol. Cell. Biol. 21: 6984-6998. PMID 11564881.
- ^ Prieto I, Suja JA, Pezzi N, Kremer L, Martínez-A C, Rufas JS, Barbero JL (2001). “Mammalian STAG3 is a cohesin specific to sister chromatid arms in meiosis I”. Nat. Cell Biol. 3: 761-766. PMID 11483963.
- ^ Lee J, Hirano T (2011). “RAD21L, a novel cohesin subunit implicated in linking homologous chromosomes in mammalian meiosis”. J. Cell Biol. 193: 263-276. PMID 21242291.
- ^ Anderson DE, Losada A, Erickson HP, Hirano T (2002). “Condensin and cohesin display different arm conformations with characteristic hinge angles”. J. Cell Biol. 156 (6): 419-424. PMID 11815634.
- ^ Haering CH, Schoffnegger D, Nishino T, Helmhart W, Nasmyth K, Löwe J. (2004). “Structure and stability of cohesin's Smc1-kleisin interaction.”. Mol. Cell 15 (6): 951-964. PMID 15383284.
- ^ Gligoris TG, Scheinost JC, Bürmann F, Petela N, Chan KL, Uluocak P, Beckouët F, Gruber S, Nasmyth K, Löwe J. (2014). “Closing the cohesin ring: structure and function of its Smc3-kleisin interface”. Science 346 (6212): 963-967. PMID 25414305.
- ^ Hara K, Zheng G, Qu Q, Liu H, Ouyang Z, Chen Z, Tomchick DR, Yu H (2014). “Structure of cohesin subcomplex pinpoints direct shugoshin-Wapl antagonism in centromeric cohesion”. Nat. Struct. Mol. Biol. 21 (10): 864-870. PMID 25173175.
- ^ Skibbens RV, Corson LB, Koshland D, Hieter P (1999). “Ctf7p is essential for sister chromatid cohesion and links mitotic chromosome structure to the DNA replication machinery”. Genes Dev 13 (3): 307-319. PMID 9990855.
- ^ Gandhi R, Gillespie PJ, Hirano T (2006). “Human Wapl is a cohesin-binding protein that promotes sister-chromatid resolution in mitotic prophase”. Curr. Biol. 16 (24): 2406-2417. PMID 17112726.
- ^ Kueng S, Hegemann B, Peters BH, Lipp JJ, Schleiffer A, Mechtler K, Peters JM (2006). “Wapl controls the dynamic association of cohesin with chromatin”. Cell 127 (5): 955-967. PMID 17113138.
- ^ Hartman T, Stead K, Koshland D, Guacci V (2000). “Pds5p is an essential chromosomal protein required for both sister chromatid cohesion and condensation in Saccharomyces cerevisiae”. J. Cell Biol. 151 (3): 613-626. PMID 11062262.
- ^ Kerrebrock AW, Moore DP, Wu JS, Orr-Weaver TL (1995). “Mei-S332, a Drosophila protein required for sister-chromatid cohesion, can localize to meiotic centromere regions”. Cell 83 (2): 247-256. PMID 7585942.
- ^ Kitajima TS, Kawashima SA, Watanabe Y (2004). “The conserved kinetochore protein shugoshin protects centromeric cohesion during meiosis”. Nature 427 (6974): 510-517. PMID 14730319.
- ^ a b Uhlmann F, Lottspeich F, Nasmyth K (1999). “Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1”. Nature 400 (6739): 37-42. PMID 10403247.
- ^ Funabiki H, Yamano H, Kumada K, Nagao K, Hunt T, Yanagida M (1996). “Cut2 proteolysis required for sister-chromatid seperation in fission yeast”. Nature 381 (6581): 438-441. PMID 8632802.
- ^ Dorsett D, Merkenschlager M (2013). “Cohesin at active genes: a unifying theme for cohesin and gene expression from model organisms to humans”. Curr Opin Cell Biol 25 (3): 327-333. PMID 23465542.
- ^ Krantz ID, McCallum J, DeScipio C, Kaur M, Gillis LA, Yaeger D, Jukofsky L, Wasserman N, Bottani A, Morris CA, Nowaczyk MJ, Toriello H, Bamshad MJ, Carey JC, Rappaport E, Kawauchi S, Lander AD, Calof AL, Li HH, Devoto M, Jackson LG (2004). “Cornelia de Lange syndrome is caused by mutations in NIPBL, the human homolog of Drosophila melanogaster Nipped-B”. Nat Genet. 36 (6): 631-635. PMID 15146186.
- ^ Tonkin ET, Wang TJ, Lisgo S, Bamshad MJ, Strachan T (2004). “NIPBL, encoding a homolog of fungal Scc2-type sister chromatid cohesion proteins and fly Nipped-B, is mutated in Cornelia de Lange syndrome”. Nat Genet. 36 (6): 636-641. PMID 15146185.
- ^ Deardorff MA, Kaur M, Yaeger D, Rampuria A, Korolev S, Pie J, Gil-Rodríguez C, Arnedo M, Loeys B, Kline AD, Wilson M, Lillquist K, Siu V, Ramos FJ, Musio A, Jackson LS, Dorsett D, Krantz ID (2007). “Mutations in cohesin complex members SMC3 and SMC1A cause a mild variant of cornelia de Lange syndrome with predominant mental retardation”. Am. J. Hum. Genet. 80 (3): 485-494. PMID 17273969.
- ^ Deardorff MA, Bando M, Nakato R, Watrin E, Itoh T, Minamino M, Saitoh K, Komata M, Katou Y, Clark D, Cole KE, De Baere E, Decroos C, Di Donato N, Ernst S, Francey LJ, Gyftodimou Y, Hirashima K, Hullings M, Ishikawa Y, Jaulin C, Kaur M, Kiyono T, Lombardi PM, Magnaghi-Jaulin L, Mortier GR, Nozaki N, Petersen MB, Seimiya H, Siu VM, Suzuki Y, Takagaki K, Wilde JJ, Willems PJ, Prigent C, Gillessen-Kaesbach G, Christianson DW, Kaiser FJ, Jackson LG, Hirota T, Krantz ID, Shirahige K (2012). “HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle”. Nature 489 (7415): 313-317. PMID 22885700.
- ^ Vega H, Waisfisz Q, Gordillo M, Sakai N, Yanagihara I, Yamada M, van Gosliga D, Kayserili H, Xu C, Ozono K, Jabs EW, Inui K, Joenje H (2005). “Roberts syndrome is caused by mutations in ESCO2, a human homolog of yeast ECO1 that is essential for the establishment of sister chromatid cohesion”. Nat Genet. 37 (5): 468-470. PMID 15821733.
- 1 コヒーシンとは
- 2 コヒーシンの概要
- 3 分裂期における機能
- 4 分裂期以外での機能
固有名詞の分類
- コヒーシンのページへのリンク