Một hệ thống đặt tên thống nhất dựa trên phát sinh chủng loại cho các biến thể histone
Tóm tắt
Các biến thể histone là các isoform protein không đồng phân có vai trò quan trọng trong việc đa dạng hóa cấu trúc nhiễm sắc. Số lượng biến thể đã biết đã tăng lên đáng kể trong những năm gần đây, nhưng sự thiếu hụt quy tắc đặt tên cho chúng đã dẫn đến nhiều phong cách đặt tên khác nhau, nhiều từ đồng nghĩa và các từ đồng âm gây nhầm lẫn, làm mờ nhạt mối quan hệ giữa các biến thể và làm phức tạp việc tìm kiếm trong cơ sở dữ liệu. Chúng tôi đề xuất một hệ thống đặt tên thống nhất cho các biến thể của cả năm loại histone, sử dụng các quy tắc đặt tên nhất quán nhưng linh hoạt để tạo ra các tên gọi có thông tin và dễ tìm kiếm. Hệ thống đặt tên này dựa trên sự sử dụng lịch sử và kết hợp các mối quan hệ phát sinh chủng loại, điều này là những dự đoán mạnh mẽ về cấu trúc và chức năng. Một đặc điểm chính là việc sử dụng dấu câu một cách nhất quán để đại diện cho sự phân rã phát sinh chủng loại, làm rõ ràng mối quan hệ giữa các kiểu biến thể mà trước đây chưa được rõ ràng. Chúng tôi khuyến nghị rằng theo mặc định, các biến thể histone mới được đặt tên với hậu tố số đại diện cho paralog của loài cụ thể mà không có ý nghĩa phát sinh chủng loại, trong khi các hậu tố chữ được dành riêng cho những nhánh biến thể có cấu trúc khác biệt. Để rõ ràng và dễ tìm kiếm, chúng tôi khuyến khích việc sử dụng các mô tả tách biệt khỏi tên biến thể dựa trên phát sinh chủng loại để chỉ ra các thuộc tính phát triển và những thuộc tính khác của các biến thể có thể độc lập với cấu trúc.
Từ khóa
Tài liệu tham khảo
Alfageme CR, Zweidler A, Mahowald A, Cohen LH: Histones of Drosophila embryos. Electrophoretic isolation and structural studies. J Biol Chem. 1974, 249: 3729-3736.
Strickland WN, Strickland M, Brandt WF, Morgan M, Von Holt C: Partial amino acid sequence of two new arginine-serine rich histones from male gonads of the sea urchin (Parechinus angulosus). FEBS Lett. 1974, 40: 161-166. 10.1016/0014-5793(74)80918-X.
Marzluff WF, Sanders LA, Miller DM, McCarty KS: Two chemically and metabolically distinct forms of calf thymus histone F3. J Biol Chem. 1972, 247: 2026-2033.
Patthy L, Smith EL: Histone III. VI. Two forms of calf thymus histone III. J Biol Chem. 1975, 250: 1919-1920.
Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ: The human and mouse replication-dependent histone genes. Genomics. 2002, 80: 487-498. 10.1006/geno.2002.6850.
Franklin SG, Zweidler A: Non-allelic variants of histones 2a, 2b and 3 in mammals. Nature. 1977, 266: 273-275. 10.1038/266273a0.
Albig W, Ebentheuer J, Klobeck G, Kunz J, Doenecke D: A solitary human H3 histone gene on chromosome 1. Hum Genet. 1996, 97: 486-491. 10.1007/BF02267072.
Schenk R, Jenke A, Zilbauer M, Wirth S, Postberg J: H3.5 is a novel hominid-specific histone H3 variant that is specifically expressed in the seminiferous tubules of human testes. Chromosoma. 2011, 120: 275-285. 10.1007/s00412-011-0310-4.
West MH, Bonner WM: Histone 2A, a heteromorphous family of eight protein species. Biochemistry. 1980, 19: 3238-3245. 10.1021/bi00555a022.
Witt O, Albig W, Doenecke D: Testis-specific expression of a novel human H3 histone gene. Exp Cell Res. 1996, 229: 301-306. 10.1006/excr.1996.0375.
Ghosh S, Klobutcher LA: A development-specific histone H3 localizes to the developing macronucleus of Euplotes. Genesis. 2000, 26: 179-188. 10.1002/(SICI)1526-968X(200003)26:3<179::AID-GENE3>3.0.CO;2-B.
Chadwick BP, Willard HF: A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome. J Cell Biol. 2001, 152: 375-384. 10.1083/jcb.152.2.375.
Bao Y, Konesky K, Park YJ, Rosu S, Dyer PN, Rangasamy D, Tremethick DJ, Laybourn PJ, Luger K: Nucleosomes containing the histone variant H2A.Bbd organize only 118 base pairs of DNA. EMBO J. 2004, 23: 3314-3324. 10.1038/sj.emboj.7600316.
Boulard M, Gautier T, Mbele GO, Gerson V, Hamiche A, Angelov D, Bouvet P, Dimitrov S: The NH2 tail of the novel histone variant H2BFWT exhibits properties distinct from conventional H2B with respect to the assembly of mitotic chromosomes. Mol Cell Biol. 2006, 26: 1518-1526. 10.1128/MCB.26.4.1518-1526.2006.
Van Doninck K, Mandigo ML, Hur JH, Wang P, Guglielmini J, Milinkovitch MC, Lane WS, Meselson M: Phylogenomics of unusual histone H2A Variants in Bdelloid rotifers. PLoS Genet. 2009, 5: e1000401-10.1371/journal.pgen.1000401.
Wiedemann SM, Mildner SN, Bonisch C, Israel L, Maiser A, Matheisl S, Straub T, Merkl R, Leonhardt H, Kremmer E, Schermelleh L, Hake SB: Identification and characterization of two novel primate-specific histone H3 variants, H3.X and H3.Y. J Cell Biol. 2010, 190: 777-791. 10.1083/jcb.201002043.
van Daal A, Elgin SC: A histone variant, H2AvD, is essential in Drosophila melanogaster. Mol Biol Cell. 1992, 3: 593-602.
Leach TJ, Mazzeo M, Chotkowski HL, Madigan JP, Wotring MG, Glaser RL: Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster. J Biol Chem. 2000, 275: 23267-23272. 10.1074/jbc.M910206199.
Miao J, Fan Q, Cui L, Li J, Li J, Cui L: The malaria parasite plasmodium falciparum histones: organization, expression, and acetylation. Gene. 2006, 369: 53-65.
Lowell JE, Kaiser F, Janzen CJ, Cross GA: Histone H2AZ dimerizes with a novel variant H2B and is enriched at repetitive DNA in Trypanosoma brucei. J Cell Sci. 2005, 118: 5721-5730. 10.1242/jcs.02688.
Siegel TN, Hekstra DR, Kemp LE, Figueiredo LM, Lowell JE, Fenyo D, Wang X, Dewell S, Cross GA: Four histone variants mark the boundaries of polycistronic transcription units in Trypanosoma brucei. Genes Dev. 2009, 23: 1063-1076. 10.1101/gad.1790409.
Dawson SC, Sagolla MS, Cande WZ: The cenH3 histone variant defines centromeres in Giardia intestinalis. Chromosoma. 2007, 116: 175-184. 10.1007/s00412-006-0091-3.
Govin J, Escoffier E, Rousseaux S, Kuhn L, Ferro M, Thevenon J, Catena R, Davidson I, Garin J, Khochbin S, Caron C: Pericentric heterochromatin reprogramming by new histone variants during mouse spermiogenesis. J Cell Biol. 2007, 176: 283-294. 10.1083/jcb.200604141.
Eirin-Lopez JM, Gonzalez-Romero R, Dryhurst D, Ishibashi T, Ausio J: The evolutionary differentiation of two histone H2A.Z variants in chordates (H2A.Z-1 and H2A.Z-2) is mediated by a stepwise mutation process that affects three amino acid residues. BMC Evol Biol. 2009, 9: 31-10.1186/1471-2148-9-31.
Bernhard D: Several highly divergent histone H3 genes are present in the hypotrichous ciliate Stylonychia lemnae. FEMS Microbiol Lett. 1999, 175: 45-50. 10.1111/j.1574-6968.1999.tb13600.x.
Postberg J, Forcob S, Chang WJ, Lipps HJ: The evolutionary history of histone H3 suggests a deep eukaryotic root of chromatin modifying mechanisms. BMC Evol Biol. 2010, 10: 259-10.1186/1471-2148-10-259.
Moosmann A, Campsteijn C, Jansen PW, Nasrallah C, Raasholm M, Stunnenberg HG, Thompson EM: Histone variant innovation in a rapidly evolving chordate lineage. BMC Evol Biol. 2011, 11: 208-10.1186/1471-2148-11-208.
Pehrson JR, Costanzi C, Dharia C: Developmental and tissue expression patterns of histone macroH2A1 subtypes. J Cell Biochem. 1997, 65: 107-113. 10.1002/(SICI)1097-4644(199704)65:1<107::AID-JCB11>3.0.CO;2-H.
Brock WA, Trostle PK, Meistrich ML: Meiotic synthesis of testis histones in the rat. Proc Natl Acad Sci U S A. 1980, 77: 371-375. 10.1073/pnas.77.1.371.
Zalensky AO, Siino JS, Gineitis AA, Zalenskaya IA, Tomilin NV, Yau P, Bradbury EM: Human testis/sperm-specific histone H2B (hTSH2B). Molecular cloning and characterization. J Biol Chem. 2002, 277: 43474-43480. 10.1074/jbc.M206065200.
Ueda K, Tanaka I: The appearance of male gamete-specific histones gH2B and gH3 during pollen development in Lilium longiflorum. Dev Biol. 1995, 169: 210-217. 10.1006/dbio.1995.1138.
Xu H, Swoboda I, Bhalla PL, Singh MB: Male gametic cell-specific expression of H2A and H3 histone genes. Plant Mol Biol. 1999, 39: 607-614. 10.1023/A:1006162120037.
Okada T, Singh MB, Bhalla PL: Histone H3 variants in male gametic cells of lily and H3 methylation in mature pollen. Plant Mol Biol. 2006, 62: 503-512. 10.1007/s11103-006-9036-8.
Pehrson JR, Fried VA: MacroH2A, a core histone containing a large nonhistone region. Science. 1992, 257: 1398-1400. 10.1126/science.1529340.
Talbert PB, Masuelli R, Tyagi AP, Comai L, Henikoff S: Centromeric localization and adaptive evolution of an Arabidopsis histone H3 variant. Plant Cell. 2002, 14: 1053-1066. 10.1105/tpc.010425.
Aul RB, Oko RJ: The major subacrosomal occupant of bull spermatozoa is a novel histone H2B variant associated with the forming acrosome during spermiogenesis. Dev Biol. 2002, 242: 376-387.
Marzluff WF, Sakallah S, Kelkar H: The sea urchin histone gene complement. Dev Biol. 2006, 300: 308-320. 10.1016/j.ydbio.2006.08.067.
Turner BM: Reading signals on the nucleosome with a new nomenclature for modified histones. Nat Struct Mol Biol. 2005, 12: 110-112. 10.1038/nsmb0205-110.
Dryhurst D, Ishibashi T, Rose KL, Eirin-Lopez JM, McDonald D, Silva-Moreno B, Veldhoen N, Helbing CC, Hendzel MJ, Shabanowitz J, Hunt DF, Ausio J: Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates. BMC Biol. 2009, 7: 86-10.1186/1741-7007-7-86.
Nei M, Rooney AP: Concerted and birth-and-death evolution of multigene families. Annu Rev Genet. 2005, 39: 121-152. 10.1146/annurev.genet.39.073003.112240.
Ingouff M, Hamamura Y, Gourgues M, Higashiyama T, Berger F: Distinct dynamics of HISTONE3 variants between the two fertilization products in plants. Curr Biol. 2007, 17: 1032-1037. 10.1016/j.cub.2007.05.019.
Ferguson L, Ellis PJ, Affara NA: Two novel mouse genes mapped to chromosome Yp are expressed specifically in spermatids. Mamm Genome. 2009, 20: 193-206. 10.1007/s00335-009-9175-8.
Talbert PB, Henikoff S: Histone variants–ancient wrap artists of the epigenome. Nat Rev Mol Cell Biol. 2010, 11: 264-275.
Huson DH, Richter DC, Rausch C, Dezulian T, Franz M, Rupp R: Dendroscope: an interactive viewer for large phylogenetic trees. BMC Bioinformatics. 2007, 8: 460-10.1186/1471-2105-8-460.
Baker RE, Rogers K: Phylogenetic analysis of fungal centromere H3 proteins. Genetics. 2006, 174: 1481-1492. 10.1534/genetics.106.062794.
Malik HS, Henikoff S: Phylogenomics of the nucleosome. Nat Struct Biol. 2003, 10: 882-891. 10.1038/nsb996.
Talbert PB, Bayes JJ, Henikoff S: The Evolution of Centromeres and Kinetochores: A Two-Part Fugue. The Kinetochore: From Molecular Discoveries to Cancer Therapy. Edited by: Wulf P, Earnshaw WC. 2008, Springer, Berlin, 193-230. 1
Tran MH, Aul RB, Xu W, van der Hoorn F, Oko R: Involvement of Classical Bipartite/Karyopherin Nuclear Import Pathway Components in Acrosomal Trafficking and Assembly During Bovine and Murid Spermiogenesis. Biol Reprod. 2012, 86: 84-10.1095/biolreprod.111.096842.
Lindsey GG, Orgeig S, Thompson P, Davies N, Maeder DL: Extended C-terminal tail of wheat histone H2A interacts with DNA of the "linker" region. J Mol Biol. 1991, 218: 805-813. 10.1016/0022-2836(91)90268-B.
Lee J, Park HS, Kim HH, Yun YJ, Lee DR, Lee S: Functional polymorphism in H2BFWT -5'UTR is associated with susceptibility to male infertility. J Cell Mol Med. 2009, 13: 1942-1951. 10.1111/j.1582-4934.2009.00830.x.
Song X, Bowen J, Miao W, Liu Y, Gorovsky M: The non-histone, N-terminal tail of an essential, chimeric H2A variant regulates mitotic H3 S10 de-phosphorylation. Genes Dev. 2012, 26: 615-629. 10.1101/gad.182683.111.
Costanzi C, Pehrson JR: MACROH2A2, a new member of the MARCOH2A core histone family. J Biol Chem. 2001, 276: 21776-21784. 10.1074/jbc.M010919200.
Waterborg JH: Dynamics of histone acetylation in vivo. A function for acetylation turnover?. Biochem Cell Biol. 2002, 80: 363-378. 10.1139/o02-080.
Waterborg JH: Evolution of histone H3: emergence of variants and conservation of post-translational modification sites. Biochem Cell Biol. 2012, 90: 79-95.
Thatcher TH, MacGaffey J, Bowen J, Horowitz S, Shapiro DL, Gorovsky MA: Independent evolutionary origin of histone H3.3-like variants of animals and Tetrahymena. Nucleic Acids Res. 1994, 22: 180-186. 10.1093/nar/22.2.180.
Waterborg JH, Robertson AJ: Common features of analogous replacement histone H3 genes in animals and plants. J Mol Evol. 1996, 43: 194-206. 10.1007/BF02338827.
Chaubet N, Clement B, Gigot C: Genes encoding a histone H3.3-like variant in Arabidopsis contain intervening sequences. J Mol Biol. 1992, 225: 569-574. 10.1016/0022-2836(92)90943-E.
Borun TW, Ajiro K, Zweidler A, Dolby TW, Stephens RE: Studies of human histone messenger RNA. II. The resolution of fractions containing individual human histone messenger RNA species. J Biol Chem. 1977, 252: 173-180.
Cui B, Liu Y, Gorovsky MA: Deposition and function of histone H3 variants in Tetrahymena thermophila. Mol Cell Biol. 2006, 26: 7719-7730. 10.1128/MCB.01139-06.
Sullivan WJ: Histone H3 and H3.3 variants in the protozoan pathogens Plasmodium falciparum and Toxoplasma gondii. DNA Seq. 2003, 14 (3): 227-231. 10.1080/1042517031000089496.
Akhmanova AS, Bindels PC, Xu J, Miedema K, Kremer H, Hennig W: Structure and expression of histone H3.3 genes in Drosophila melanogaster and Drosophila hydei. Genome. 1995, 38: 586-600. 10.1139/g95-075.
Rando OJ: Genome-wide measurement of histone H3 replacement dynamics in yeast. Methods Mol Biol. 2011, 759: 41-60. 10.1007/978-1-61779-173-4_3.
Chrom DB: The Chromatin Database. [http://www.chromdb.org]
Okada T, Endo M, Singh MB, Bhalla PL: Analysis of the histone H3 gene family in Arabidopsis and identification of the male-gamete-specific variant AtMGH3. Plant J. 2005, 44: 557-568. 10.1111/j.1365-313X.2005.02554.x.
Earnshaw WC, Rothfield N: Identification of a family of human centromere proteins using autoimmune sera from patients with scleroderma. Chromosoma. 1985, 91: 313-321. 10.1007/BF00328227.
Stoler S, Keith KC, Curnick KE, Fitzgerald-Hayes M: A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis. Genes Dev. 1995, 9: 573-586. 10.1101/gad.9.5.573.
Dalmasso MC, Onyango DO, Naguleswaran A, Sullivan WJ, Angel SO: Toxoplasma H2A variants reveal novel insights into nucleosome composition and functions for this histone family. J Mol Biol. 2009, 392: 33-47. 10.1016/j.jmb.2009.07.017.
Ishibashi T, Li A, Eirin-Lopez JM, Zhao M, Missiaen K, Abbott DW, Meistrich M, Hendzel MJ, Ausio J: H2A.Bbd: an X-chromosome-encoded histone involved in mammalian spermiogenesis. Nucleic Acids Res. 2010, 38: 1780-1789. 10.1093/nar/gkp1129.
Soboleva TA, Nekrasov M, Pahwa A, Williams R, Huttley GA, Tremethick DJ: A unique H2A histone variant occupies the transcriptional start site of active genes. Nat Struct Mol Biol. 2011, 19: 25-30. 10.1038/nsmb.2161.
Syed SH, Boulard M, Shukla MS, Gautier T, Travers A, Bednar J, Faivre-Moskalenko C, Dimitrov S, Angelov D: The incorporation of the novel histone variant H2AL2 confers unusual structural and functional properties of the nucleosome. Nucleic Acids Res. 2009, 37: 4684-4695. 10.1093/nar/gkp473.
Kasinsky HE, Lewis JD, Dacks JB, Ausio J: Origin of H1 linker histones. FASEB J. 2001, 15 (1): 34-42. 10.1096/fj.00-0237rev.
Kinkade JM, Cole RD: The resolution of four lysine-rich histones derived from calf thymus. J Biol Chem. 1966, 241: 5790-5797.
Kinkade JM, Cole RD: A structural comparison of different lysine-rich histones of calf thymus. J Biol Chem. 1966, 241: 5798-5805.
Happel N, Doenecke D: Histone H1 and its isoforms: contribution to chromatin structure and function. Gene. 2009, 431: 1-12. 10.1016/j.gene.2008.11.003.
Izzo A, Kamieniarz K, Schneider R: The histone H1 family: specific members, specific functions?. Biol Chem. 2008, 389: 333-343.
Seyedin SM, Kistler WS: H1 histone subfractions of mammalian testes. 1. Organ specificity in the rat. Biochemistry. 1979, 18: 1371-1375. 10.1021/bi00574a038.
Lennox RW, Cohen LH: The histone H1 complements of dividing and nondividing cells of the mouse. J Biol Chem. 1983, 258: 262-268.
Lennox RW, Cohen LH: The alterations in H1 histone complement during mouse spermatogenesis and their significance for H1 subtype function. Dev Biol. 1984, 103: 80-84. 10.1016/0012-1606(84)90009-5.
Parseghian MH, Henschen AH, Krieglstein KG, Hamkalo BA: A proposal for a coherent mammalian histone H1 nomenclature correlated with amino acid sequences. Protein Sci. 1994, 3: 575-587.
Albig W, Kardalinou E, Drabent B, Zimmer A, Doenecke D: Isolation and characterization of two human H1 histone genes within clusters of core histone genes. Genomics. 1991, 10: 940-948. 10.1016/0888-7543(91)90183-F.
Albig W, Drabent B, Kunz J, Kalff-Suske M, Grzeschik KH, Doenecke D: All known human H1 histone genes except the H1(0) gene are clustered on chromosome 6. Genomics. 1993, 16: 649-654. 10.1006/geno.1993.1243.
Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D: Human histone gene organization: nonregular arrangement within a large cluster. Genomics. 1997, 40: 314-322. 10.1006/geno.1996.4592.
Peretti M, Khochbin S: The evolution of the differentiation-specific histone H1 gene basal promoter. J Mol Evol. 1997, 44: 128-134. 10.1007/PL00006129.
Brocard MP, Triebe S, Peretti M, Doenecke D, Khochbin S: Characterization of the two H1(zero)-encoding genes from Xenopus laevis. Gene. 1997, 189: 127-134. 10.1016/S0378-1119(96)00845-1.
Eirín-López JM, González-Tizón AM, Martinez A, Méndez J: Molecular and evolutionary analysis of mussel histone genes (Mytilus spp.): possible evidence of an "orphon origin" for H1 histone genes. J Mol Evol. 2002, 55: 272-283. 10.1007/s00239-002-2325-1.
González-Romero R, Ausió J, Méndez J, Eirín-López JM: Early evolution of histone genes: prevalence of an 'orphon' H1 lineage in protostomes and birth-and-death process in the H2A family. J Mol Evol. 2008, 66: 505-518. 10.1007/s00239-008-9109-1.
González-Romero R, Ausió J, Méndez J, Eirín-López JM: Histone genes of the razor clam Solen marginatus unveil new aspects of linker histone evolution in protostomes. Genome. 2009, 52: 597-607. 10.1139/G09-034.
Garel A, Mazen A, Champagne M, Sautiere P, Kmiecik D, Loy O, Biserte G: Chicken erythrocyte histone H5; I. Amino terminal sequence (70 residues). FEBS Lett. 1975, 50: 195-199. 10.1016/0014-5793(75)80487-X.
Khochbin S: Histone H1 diversity: bridging regulatory signals to linker histone function. Gene. 2001, 271: 1-12. 10.1016/S0378-1119(01)00495-4.
Smith BJ, Walker JM, Johns EW: Structural homology between a mammalian H1(0) subfraction and avian erythrocyte-specific histone H5. FEBS Lett. 1980, 112: 22-24.
Lieber T, Angerer LM, Angerer RC, Childs G: A histone H1 protein in sea urchins is encoded by a poly(A) + mRNA. Proc Natl Acad Sci U S A. 1988, 85: 4123-4127. 10.1073/pnas.85.12.4123.
Ohe Y, Hayashi H, Iwai K: Human spleen histone H1. Isolation and amino acid sequences of three minor variants, H1a, H1c, and H1d. J Biochem. 1989, 106: 844-857.
Parseghian MH, Clark RF, Hauser LJ, Dvorkin N, Harris DA, Hamkalo BA: Fractionation of human H1 subtypes and characterization of a subtype-specific antibody exhibiting non-uniform nuclear staining. Chromosome Res. 1993, 1: 127-139. 10.1007/BF00710036.