HIST1H2AL: Difference between revisions
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{{ | '''Histone H2A type 1''' is a [[protein]] that in humans is encoded by the ''HIST1H2AL'' [[gene]].<ref name="pmid9439656">{{cite journal |vauthors=Albig W, Doenecke D | title = The human histone gene cluster at the D6S105 locus | journal = Hum Genet | volume = 101 | issue = 3 | pages = 284–94 |date=Feb 1998 | pmid = 9439656 | pmc = | doi =10.1007/s004390050630 }}</ref><ref name="pmid9031620">{{cite journal |vauthors=Albig W, Meergans T, Doenecke D | title = Characterization of the H1.5 gene completes the set of human H1 subtype genes | journal = Gene | volume = 184 | issue = 2 | pages = 141–8 |date=Mar 1997 | pmid = 9031620 | pmc = | doi =10.1016/S0378-1119(96)00582-3 }}</ref><ref name="pmid12408966">{{cite journal |vauthors=Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ | title = The human and mouse replication-dependent histone genes | journal = Genomics | volume = 80 | issue = 5 | pages = 487–98 |date=Oct 2002 | pmid = 12408966 | pmc = | doi =10.1016/S0888-7543(02)96850-3 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HIST1H2AL histone cluster 1, H2al| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8332| accessdate = }}</ref> | ||
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| summary_text = Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H2AL histone cluster 1, H2al| url = | | summary_text = Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H2AL histone cluster 1, H2al| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8332| accessdate = }}</ref> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal |vauthors=Du Clos TW, Zlock LT, Marnell L |title=Definition of a C-reactive protein binding determinant on histones. |journal=J. Biol. Chem. |volume=266 |issue= 4 |pages= 2167–71 |year= 1991 |pmid= 1989977 |doi= }} | ||
*{{cite journal | | *{{cite journal |vauthors=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535–44 |year= 1998 |pmid= 9566873 |doi= 10.1128/mcb.18.5.2535| pmc=110633 }} | ||
*{{cite journal |vauthors=Zhang Y, Sun ZW, Iratni R, etal |title=SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex. |journal=Mol. Cell |volume=1 |issue= 7 |pages= 1021–31 |year= 1998 |pmid= 9651585 |doi=10.1016/S1097-2765(00)80102-1 }} | |||
*{{cite journal |vauthors=Carrier F, Georgel PT, Pourquier P, etal |title=Gadd45, a p53-responsive stress protein, modifies DNA accessibility on damaged chromatin. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 1673–85 |year= 1999 |pmid= 10022855 |doi= | pmc=83961 }} | |||
*{{cite journal | *{{cite journal |vauthors=Albig W, Trappe R, Kardalinou E, etal |title=The human H2A and H2B histone gene complement. |journal=Biol. Chem. |volume=380 |issue= 1 |pages= 7–18 |year= 1999 |pmid= 10064132 |doi=10.1515/BC.1999.002 }} | ||
*{{cite journal | *{{cite journal |vauthors=Deng L, de la Fuente C, Fu P, etal |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. |journal=Virology |volume=277 |issue= 2 |pages= 278–95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593 }} | ||
*{{cite journal | *{{cite journal |vauthors=Deng L, Wang D, de la Fuente C, etal |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA. |journal=Virology |volume=289 |issue= 2 |pages= 312–26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129 }} | ||
*{{cite journal | *{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }} | ||
*{{cite journal | *{{cite journal |vauthors=Kzhyshkowska J, Rusch A, Wolf H, Dobner T |title=Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7. |journal=Biochem. J. |volume=371 |issue= Pt 2 |pages= 385–93 |year= 2003 |pmid= 12489984 |doi= 10.1042/BJ20021281 | pmc=1223277 }} | ||
*{{cite journal | *{{cite journal |vauthors=Lusic M, Marcello A, Cereseto A, Giacca M |title=Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6550–61 |year= 2004 |pmid= 14657027 |doi= 10.1093/emboj/cdg631 | pmc=291826 }} | ||
*{{cite journal | | |||
*{{cite journal | | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=8332}} | |||
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Latest revision as of 13:38, 31 August 2017
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Histone H2A type 1 is a protein that in humans is encoded by the HIST1H2AL gene.[1][2][3][4]
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.[4]
References
- ↑ Albig W, Doenecke D (Feb 1998). "The human histone gene cluster at the D6S105 locus". Hum Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656.
- ↑ Albig W, Meergans T, Doenecke D (Mar 1997). "Characterization of the H1.5 gene completes the set of human H1 subtype genes". Gene. 184 (2): 141–8. doi:10.1016/S0378-1119(96)00582-3. PMID 9031620.
- ↑ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- ↑ 4.0 4.1 "Entrez Gene: HIST1H2AL histone cluster 1, H2al".
Further reading
- Du Clos TW, Zlock LT, Marnell L (1991). "Definition of a C-reactive protein binding determinant on histones". J. Biol. Chem. 266 (4): 2167–71. PMID 1989977.
- El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter". Mol. Cell. Biol. 18 (5): 2535–44. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
- Zhang Y, Sun ZW, Iratni R, et al. (1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell. 1 (7): 1021–31. doi:10.1016/S1097-2765(00)80102-1. PMID 9651585.
- Carrier F, Georgel PT, Pourquier P, et al. (1999). "Gadd45, a p53-responsive stress protein, modifies DNA accessibility on damaged chromatin". Mol. Cell. Biol. 19 (3): 1673–85. PMC 83961. PMID 10022855.
- Albig W, Trappe R, Kardalinou E, et al. (1999). "The human H2A and H2B histone gene complement". Biol. Chem. 380 (1): 7–18. doi:10.1515/BC.1999.002. PMID 10064132.
- Deng L, de la Fuente C, Fu P, et al. (2001). "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones". Virology. 277 (2): 278–95. doi:10.1006/viro.2000.0593. PMID 11080476.
- Deng L, Wang D, de la Fuente C, et al. (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA". Virology. 289 (2): 312–26. doi:10.1006/viro.2001.1129. PMID 11689053.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Kzhyshkowska J, Rusch A, Wolf H, Dobner T (2003). "Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7". Biochem. J. 371 (Pt 2): 385–93. doi:10.1042/BJ20021281. PMC 1223277. PMID 12489984.
- Lusic M, Marcello A, Cereseto A, Giacca M (2004). "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter". EMBO J. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
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