Histones

Abstract

Histones, the major protein constituents of the eukaryotic chromosomes, are small proteins that are enriched in basic amino acids and highly conserved in evolution. They are classified either on the basis of their content of basic amino acids as very lysine rich (H1), moderately lysine rich (H2A and H2B) and arginine rich (H3 and H4), or in respect to their position in the nucleosome as linker or core histones.

Keywords: histones; replacement histones; histone genes; gene cluster; pseudogenes

Figure 1.

General organization of histone proteins. All five histones consist of a globular domain (indicated as circles) and extended, flexible protein portions. In core histones, the structured domain consists of the histone fold motif and adjacent α‐helix structures. The length of the individual portions is given in amino acid numbers, the numbers of lysine (K) and arginine (R) residues is indicated for each domain (in parentheses). Due to slight differences within the H1 family, ranging from 193 (H1°) to 220 amino acid residues (H1.3), average numbers are given; the lysine (K) and arginine (R) data refer to the human subtype H1.2. The core histone domain dimensions are based on crystallographic data (Luger et al., ) and human histone sequences (Albig and Doenecke, ). The N‐terminal domains of the core histones contain multiple sites for posttranslational modification by acetylation, methylation or phosphorylation.

Figure 2.

Distribution of histone genes within the two clusters on the short arm of human chromosome 6 and on the long arm of chromosome 1. The bars indicate histone genes in their order of arrangement at the 6p21.3–22 and the 1q21 locus. The only known nonhistone gene within the clusters is the hemochromatosis (HFE) gene that is mutated in most cases of hemochromatosis, an iron storage disease. Histone pseudogenes are presented as dotted lines. Mb (megabases) = 106 deoxynucleotide pairs; kb (kilobases) = 103 deoxynucleotide pairs; cen and ter indicate the orientation (centromeric versus telomeric) of the cluster. The orientation of the cluster on chromosome 1 and the distance between its two subgroups of histone genes are unknown.

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References

Albig W and Doenecke D (1997) The human histone gene cluster at the D6S105 locus. Human Genetics 101: 284–294.

Arents G, Burlingame RW, Wang BW, Love WE and Moudrianakis EN (1991) The nucleosomal core histone octamer at 3.1 Å resolution: a tripartite protein assembly and a left‐handed superhelix. Proceedings of the National Academy of Sciences of the United States of America 88: 10148–10152.

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Costanzi C, Stein P, Worrad DM, Schultz RM and Pehrson JR (2000) Histone macroH2A1 is concentrated in the inactive X chromosome of female pre‐implantation mouse embryos. Development 127: 2283–2289.

Dominski Z and Marzluff WF (1999) Formation of the 3′ end of histone mRNA. Gene 239: 1–14.

Luger K, Mader AW, Richmond RK, Sargent DF and Richmond TJ (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389: 251–260.

Ramsey‐Ewing A, van Wijnen AJ, Stein GS and Stein JL (1994) Delineation of a human histone H4 cell cycle element in vivo: the master switch for H4 gene transcription. Proceedings of the National Academy of Sciences of the United States of America 91: 4475–4479.

Trappe R, Doenecke D and Albig W (1999) The expression of human H2A‐H2 histone gene pairs is regulated by multiple sequence elements in their joint promoters. Biochimica et Biophysica Acta 1446: 341–351.

Wells D, Hoffman D and Kedes L (1987) Unusual structure, evolutionary conservation of non‐coding sequences and numerous pseudogenes characterize the human H3.3 histone multigene family. Nucleic Acids Research 15: 2871–2889.

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Further Reading

Albig W and Doenecke D (1997) The human histone gene cluster at the D6S105 locus. Human Genetics 101: 284–294.

Albig W, Kioschis P, Poustka A, Meergans K and Doenecke D (1997) Human histone gene organization: nonregular arrangement within a large cluster. Genomics 40: 314–322.

Drabent B, Saftig P, Bode C and Doenecke D (2000) Spermatogenesis proceeds normally in mice without linker histone H1t. Histochemistry and Cell Biology 113: 433–442.

Kasinsky HE, Lewis JD, Dacks JB and Ausio J (2001) Origin of H1 linker histones. FASEB Journal 15: 34–42.

Khochbin S and Wolffe AP (1994) Developmentally regulated expression of linker histone variants in vertebrates. European Journal of Biochemistry 225: 501–510.

Osley MA (1991) The regulation of histone synthesis in the cell cycle. Annual Review of Biochemistry 60: 827–861.

Rabini S, Franke K, Saftig P, et al. (2000) Spermatogenesis in mice is not affected by histone H1.1 deficiency. Experimental Cell Research 255: 114–124.

Sirotkin AM, Edelmann W, Cheng G, et al. (1995) Mice develop normally without the H1° linker histone. Proceedings of the National Academy of Sciences of the United States of America 92: 6434–6438.

Wolffe A (1998) Chromatin: Structure and Function. San Diego, CA: Academic Press.

Wolffe AP, Khochbin S and Dimitrov S (1997) What do linker histones do in chromatin? BioEssays 19: 249–255.

Web Links

H1 histone family, member 0 (H1F0); Locus ID: 3005. LocusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?1=3005

H1 histone family, member T (testis‐specific) (H1FT); Locus ID: 3010. locusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?1=3010

H2A histone family, member X (H2AFX); Locus ID: 3014. LocusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?1=3014

H3 histone, family 3A (H3F3A); Locus ID: 3020. LocusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?1=3020

H4 histone family, member N (H4FN); Locus ID: 8370. locusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?1=8370

H1 histone family, member 0 (H1F0); MIM number: 142708. OMIM: http://www.ncbi.nlm.nih.gov/htbin‐post/Omim/dispmim?142708

H1 histone family, member T (testis‐specific) (H1FT); MIM number: 142712. OMIM: http://www.ncbi.nlm.nih.gov/htbin‐post/Omim/dispmim?142712

H2A histone family, member X (H2AFX); MIM number: 601772. OMIM: http://www3.ncbi.nlm.nih.gov/htbin‐post/Omim/dispmim?601772

H3 histone, family 3A (H3F3A); MIM number: 601128. OMIM: http://www.ncbi.nlm.nih.gov/htbin‐post/Omim/dispmim?601128

H4 histone family, member N (H4FN); MIM number: 605050. OMIM: http://www.ncbi.nlm.nih.gov/htbin‐post/Omim/dispmim?605050

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How to Cite close
Doenecke, Detlef, and Albig, Werner(Jan 2006) Histones. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0005908]