The family of
Heterochromatin Protein 1 (HP1) ("Chromobox Homolog", CBX) consists of highly conserved proteins, which have important functions in the cell nucleus. These functions include gene repression by heterochromatin formation, transcriptional activation, regulation of binding of cohesion complexes to centromere, sequesteration of genes to nuclear periphery, transcriptional arrest, maintenance of heterochromatin integrity, gene repression at single nucleosome level and gene repression by heterochromatization of euchromatin. HP1 proteins are fundamental units of heterochromatin packaging that are enriched at the centromeres and telomeres of nearly all Eukaryotic chromosomes with the notable exception of budding yeast, in which a yeast-specific silencing complex of SIR (silent information regulatory) proteins serve a similar function. Members of the HP1 family are characterized by an N-terminal chromodomain and a C-terminal chromoshadow domain, separated by a Hinge region. HP1 is also found at euchromatic sites, where its binding correlates with gene repression. HP1 was originally discovered byTharappel C James and Sarah Elgin in 1986 as a factor in the phenomenon known as position effect variegation in Drosophila melanogaster. [1 ] [2 ]
Paralogs and Orthologs [ edit ]
paralogs of HP1 are found in Drosophila melanogaster, HP1a, HP1b and HP1c. Subsequently orthologs of HP1 were also discovered in S. pombe (Swi6), Xenopus (Xhp1α and Xhp1γ) and Chicken (CHCB1, CHCB2 and CHCB3). In mammals, there are three [3 ] paralogs: HP1α, HP1β and HP1γ.
HP1β in mammals [ edit ]
HP1β interacts with the Histone-
Methyltransferase (HMTase) Suv(3-9)h1 and is a component of both pericentric and telomeric heterochromatin. [4 ] [5 ] HP1β is a dosage-dependent modifier of pericentric heterochromatin-induced silencing [6 ] and silencing is thought to involve a dynamic association of the HP1β [7 ] chromodomain with the tri-methylated Histone H3 Me(3)K9H3.
HP1 Interacting Proteins [ edit ]
HP1 seems to interact with numerous other proteins/molecules with different cellular functions in different organisms. Some of these HP1 interacting partners are:
Histone H1, Histone H3, Methylated K9 Histone H3, Histone H4, Histone methyltransferase, DNA methyltransferase, Methyl CpG binding protein MeCP2, and the origin recognition complex protein ORC2
See also [ edit ]
References [ edit ]
^ James, T.C. & S.C Elgin (1986). "Identification of a nonhistone chromosomal protein associated with heterochromatin in Drosophila melanogaster and its gene". Mol. Cell. Biol. 6 (11): 3862–3872. PMC 367149. PMID 3099166.
^ Eissenberg, J.C., James, T.C., Foster-Hartnett, D.M., Hartnett, T., Ngan, V.K.W., Craig, C., Elgin, S.C.R. (1990). "Mutation in a heterochromatin-specific chromosomal protein is associated with suppression of position-effect variegation in Drosophila melanogaster". Proceedings of the National Academy of Sciences of the United States of America 87 (24): 9923–7. doi: 10.1073/pnas.87.24.9923. PMC 55286. PMID 2124708.
^ Singh PB, Miller JR, Pearce J, Kothary R, Burton RD, Paro R, James TC, Gaunt SJ. (February 1991). "A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants". Nucleic Acids Res. 19 (4): 789–94. doi: 10.1093/nar/19.4.789. PMC 333712. PMID 1708124.
^ Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T. (April 1999). "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31". EMBO J. 18 (7): 1923–38. doi: 10.1093/emboj/18.7.1923. PMC 1171278. PMID 10202156.
^ Wreggett KA, Hill F, James PS, Hutchings A, Butcher GW, Singh PB (1994). "A mammalian homologue of Drosophila heterochromatin protein 1 (HP1) is a component of constitutive heterochromatin". Cytogenet. Cell Genet. 66 (2): 99–103. doi: 10.1159/000133676. PMID 8287692.
^ Sharma GG, Hwang KK, Pandita RK, Gupta A, Dhar S, Parenteau J, Agarwal M, Worman HJ, Wellinger RJ, Pandita TK. (Nov; 2003). "Human Heterochromatin Protein 1 Isoforms HP1Hsα and HP1Hsβ Interfere with hTERT-Telomere Interactions and Correlate with Changes in Cell Growth and Response to Ionizing Radiation". Mol. Cell. Biol. 23 (22): 8363–76. doi: 10.1128/MCB.23.22.8363-8376.2003. PMC 262350. PMID 14585993.
^ Festenstein R, Sharghi-Namini S, Fox M, Roderick K, Tolaini M, Norton T, Saveliev A, Kioussis D, Singh P (December 1999). "Heterochromatin protein 1 modifies mammalian PEV in a dose- and chromosomal-context-dependent manner". Nat. Genet. 23 (4): 457–61. doi: 10.1038/70579. PMID 10581035.
Further reading [ edit ]
β-Scaffold factors with minor groove contacts
(0) Other transcription factors
transcription factor/coregulator deficiencies B bsyn: dna ( repl, cycl, reco, repr) · tscr ( fact, tcrg, nucl, rnat, rept, ptts) · tltn ( risu, pttl, nexn) · dnab, rnab/ runp · stru ( domn, 1°, 2°, 3°, 4°)