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'''Elongator complex protein 3''', also named KAT9, is a [[protein]] that in humans is encoded by the ''ELP3'' [[gene]].<ref name="pmid11714725">{{cite journal | vauthors = Hawkes NA, Otero G, Winkler GS, Marshall N, Dahmus ME, Krappmann D, Scheidereit C, Thomas CL, Schiavo G, Erdjument-Bromage H, Tempst P, Svejstrup JQ | title = Purification and characterization of the human elongator complex | journal = J Biol Chem | volume = 277 | issue = 4 | pages = 3047–52 |date=Jan 2002 | pmid = 11714725 | pmc =  | doi = 10.1074/jbc.M110445200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ELP3 elongation protein 3 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55140| accessdate = }}</ref> ELP3 is the catalytic [[histone acetyltransferase]] subunit of the [[RNA polymerase]] II elongator complex, which is a component of the [[RNA polymerase]] II (Pol II) [[holoenzyme]] and is involved in transcriptional elongation. ELP3 supports the migration and branching of projection neurons through acetylation of alpha-tubulin in the developing [[cerebral cortex]].<ref>{{cite journal | vauthors = Creppe C, Malinouskaya L, Volvert ML, Gillard M, Close P, Malaise O, Laguesse S, Cornez I, Rahmouni S, Ormenese S, Belachew S, Malgrange B, Chapelle JP, Siebenlist U, Moonen G, Chariot A, Nguyen L | title = Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin | journal = Cell | volume = 136 | issue = 3 | pages = 551–64 | date = Feb 2009 | pmid = 19185337 | doi = 10.1016/j.cell.2008.11.043 | access-date =  }}</ref> In mammals, ELP3 is important for paternal [[DNA demethylation]] after fertilization.<ref>{{cite journal | vauthors = Okada Y, Yamagata K, Hong K, Wakayama T, Zhang Y | title = A role for the elongator complex in zygotic paternal genome demethylation | journal = Nature | volume = 463 | issue = 7280 | pages = 554–8 | date = Jan 2010 | pmid = 20054296 | doi = 10.1038/nature08732 | pmc=2834414}}</ref> ELP3 is potentially involved in cellular redox homeostasis by mediating the acetylation of [[glucose-6-phosphate dehydrogenase]].<ref>{{cite journal | vauthors = Wang YP, Zhou LS, Zhao YZ, Wang SW, Chen LL, Liu LX, Ling ZQ, Hu FJ, Sun YP, Zhang JY, Yang C, Yang Y, Xiong Y, Guan KL, Ye D | title = Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress | journal = The EMBO Journal | volume = 33 | issue = 12 | pages = 1304–20 | date = Jun 2014 | pmid = 24769394 | doi = 10.1002/embj.201387224 | pmc=4194121}}</ref> Besides, ELP3 may play a role in [[chromatin remodeling]] and is involved in acetylation of [[Histone H3|histones H3]] and probably H4.
'''Elongator complex protein 3''', also named KAT9, is a [[protein]] that in humans is encoded by the ''ELP3'' [[gene]].<ref name="pmid11714725">{{cite journal | vauthors = Hawkes NA, Otero G, Winkler GS, Marshall N, Dahmus ME, Krappmann D, Scheidereit C, Thomas CL, Schiavo G, Erdjument-Bromage H, Tempst P, Svejstrup JQ | title = Purification and characterization of the human elongator complex | journal = J Biol Chem | volume = 277 | issue = 4 | pages = 3047–52 |date=Jan 2002 | pmid = 11714725 | pmc =  | doi = 10.1074/jbc.M110445200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ELP3 elongation protein 3 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55140| accessdate = }}</ref> ELP3 is the catalytic [[histone acetyltransferase]] subunit of the [[RNA polymerase]] II elongator complex, which is a component of the RNA polymerase II (Pol II) [[holoenzyme]] and is involved in transcriptional elongation. ELP3 supports the migration and branching of [[projection neuron]]s through [[acetylation]] of alpha-tubulin in the developing [[cerebral cortex]].<ref>{{cite journal | vauthors = Creppe C, Malinouskaya L, Volvert ML, Gillard M, Close P, Malaise O, Laguesse S, Cornez I, Rahmouni S, Ormenese S, Belachew S, Malgrange B, Chapelle JP, Siebenlist U, Moonen G, Chariot A, Nguyen L | title = Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin | journal = Cell | volume = 136 | issue = 3 | pages = 551–64 | date = Feb 2009 | pmid = 19185337 | doi = 10.1016/j.cell.2008.11.043 | access-date =  }}</ref> In mammals, ELP3 is important for paternal [[DNA demethylation]] after [[Fertilisation|fertilization]].<ref>{{cite journal | vauthors = Okada Y, Yamagata K, Hong K, Wakayama T, Zhang Y | title = A role for the elongator complex in zygotic paternal genome demethylation | journal = Nature | volume = 463 | issue = 7280 | pages = 554–8 | date = Jan 2010 | pmid = 20054296 | doi = 10.1038/nature08732 | pmc=2834414}}</ref> ELP3 is potentially involved in cellular redox [[homeostasis]] by mediating the acetylation of [[glucose-6-phosphate dehydrogenase]].<ref>{{cite journal | vauthors = Wang YP, Zhou LS, Zhao YZ, Wang SW, Chen LL, Liu LX, Ling ZQ, Hu FJ, Sun YP, Zhang JY, Yang C, Yang Y, Xiong Y, Guan KL, Ye D | title = Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress | journal = The EMBO Journal | volume = 33 | issue = 12 | pages = 1304–20 | date = Jun 2014 | pmid = 24769394 | doi = 10.1002/embj.201387224 | pmc=4194121}}</ref> Besides, ELP3 may play a role in [[chromatin remodeling]] and is involved in acetylation of [[Histone H3|histones H3]] and probably [[Histone H4|H4]].
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*{{cite journal  | vauthors=Rengo F, Brevetti G, Piscione F |title=[Behavior of some metabolic parameters during post-ischemic and post-contraction vasodilation in normal subjects] |journal=Bollettino della Società italiana di cardiologia |volume=20 |issue= 12 |pages= 1801–6 |year= 1977 |pmid= 10936 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Rengo F, Brevetti G, Piscione F |title=[Behavior of some metabolic parameters during post-ischemic and post-contraction vasodilation in normal subjects] |journal=Bollettino della Società italiana di cardiologia |volume=20 |issue= 12 |pages= 1801–6 |year= 1977 |pmid= 10936 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | vauthors=Ninomiya Y, Okada M, Kotomura N |title=Genomic organization and isoforms of the mouse ELP gene. |journal=J. Biochem. |volume=118 |issue= 2 |pages= 380–9 |year= 1996 |pmid= 8543574 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Ninomiya Y, Okada M, Kotomura N |title=Genomic organization and isoforms of the mouse ELP gene. |journal=J. Biochem. |volume=118 |issue= 2 |pages= 380–9 |year= 1996 |pmid= 8543574 |doi=  10.1093/oxfordjournals.jbchem.a124918|display-authors=etal}}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  | vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948  }}
*{{cite journal  | vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948  }}

Latest revision as of 08:47, 10 January 2019

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SpeciesHumanMouse
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RefSeq (protein)

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Elongator complex protein 3, also named KAT9, is a protein that in humans is encoded by the ELP3 gene.[1][2] ELP3 is the catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. ELP3 supports the migration and branching of projection neurons through acetylation of alpha-tubulin in the developing cerebral cortex.[3] In mammals, ELP3 is important for paternal DNA demethylation after fertilization.[4] ELP3 is potentially involved in cellular redox homeostasis by mediating the acetylation of glucose-6-phosphate dehydrogenase.[5] Besides, ELP3 may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4.


References

  1. Hawkes NA, Otero G, Winkler GS, Marshall N, Dahmus ME, Krappmann D, Scheidereit C, Thomas CL, Schiavo G, Erdjument-Bromage H, Tempst P, Svejstrup JQ (Jan 2002). "Purification and characterization of the human elongator complex". J Biol Chem. 277 (4): 3047–52. doi:10.1074/jbc.M110445200. PMID 11714725.
  2. "Entrez Gene: ELP3 elongation protein 3 homolog (S. cerevisiae)".
  3. Creppe C, Malinouskaya L, Volvert ML, Gillard M, Close P, Malaise O, Laguesse S, Cornez I, Rahmouni S, Ormenese S, Belachew S, Malgrange B, Chapelle JP, Siebenlist U, Moonen G, Chariot A, Nguyen L (Feb 2009). "Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin". Cell. 136 (3): 551–64. doi:10.1016/j.cell.2008.11.043. PMID 19185337.
  4. Okada Y, Yamagata K, Hong K, Wakayama T, Zhang Y (Jan 2010). "A role for the elongator complex in zygotic paternal genome demethylation". Nature. 463 (7280): 554–8. doi:10.1038/nature08732. PMC 2834414. PMID 20054296.
  5. Wang YP, Zhou LS, Zhao YZ, Wang SW, Chen LL, Liu LX, Ling ZQ, Hu FJ, Sun YP, Zhang JY, Yang C, Yang Y, Xiong Y, Guan KL, Ye D (Jun 2014). "Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress". The EMBO Journal. 33 (12): 1304–20. doi:10.1002/embj.201387224. PMC 4194121. PMID 24769394.

Further reading