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A Unified Phylogeny-based Nomenclature for Histone Variants

Abstract

Histone variants are non-allelic protein isoforms that play key roles in diversifying chromatin structure. The known number of such variants has greatly increased in recent years, but the lack of naming conventions for them has led to a variety of naming styles, multiple synonyms and misleading homographs that obscure variant relationships and complicate database searches. We propose here a unified nomenclature for variants of all five classes of histones that uses consistent but flexible naming conventions to produce names that are informative and readily searchable. The nomenclature builds on historical usage and incorporates phylogenetic relationships, which are strong predictors of structure and function. A key feature is the consistent use of punctuation to represent phylogenetic divergence, making explicit the relationships among variant subtypes that have previously been implicit or unclear. We recommend that by default new histone variants be named with organism-specific paralog-number suffixes that lack phylogenetic implication, while letter suffixes be reserved for structurally distinct clades of variants. For clarity and searchability, we encourage the use of descriptors that are separate from the phylogeny-based variant name to indicate developmental and other properties of variants that may be independent of structure.

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References
1.
Pehrson J, Costanzi C, Dharia C . Developmental and tissue expression patterns of histone macroH2A1 subtypes. J Cell Biochem. 1997; 65(1):107-13. DOI: 10.1002/(sici)1097-4644(199704)65:1<107::aid-jcb11>3.0.co;2-h. View

2.
Happel N, Doenecke D . Histone H1 and its isoforms: contribution to chromatin structure and function. Gene. 2008; 431(1-2):1-12. DOI: 10.1016/j.gene.2008.11.003. View

3.
Gonzalez-Romero R, Ausio J, Mendez J, Eirin-Lopez J . Histone genes of the razor clam Solen marginatus unveil new aspects of linker histone evolution in protostomes. Genome. 2009; 52(7):597-607. DOI: 10.1139/G09-034. View

4.
Smith B, Walker J, JOHNS E . Structural homology between a mammalian H1(0) subfraction and avian erythrocyte-specific histone H5. FEBS Lett. 1980; 112(1):42-4. DOI: 10.1016/0014-5793(80)80122-0. View

5.
Tran M, Aul R, 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. 2011; 86(3):84. DOI: 10.1095/biolreprod.111.096842. View