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Acetylation

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  • First Online:
Encyclopedia of AIDS
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Definition

Acetylation is a protein post translational modification (PTM) catalyzed by a family of cellular enzymes named histone acetyltransferases (HATs). HATs catalyze the transfer of an acetyl group from the acetyl coenzyme A (acetyl-CoA) to the ε-amine group of specific lysine residues of protein substrates. The addition of an acetyl group alters the positive charge of specific lysines, thus modifying the electrostatic properties of the proteins targeted by HATs. The protein chemical modification occurring following acetylation results in modified protein functions. Proteins modified by acetylation might be both of cellular or viral origins.

The Diversity of HATs

Acetylation together with other types of PTMs (e.g., sumoylation, phosphorylation) extends the range of possible molecular structures beyond the limits imposed by the twenty encoded amino acids and, if reversible, gives a means of control and signaling.

In the past decades, protein acetylation has been widely explored...

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References

  • Allouch A, Cereseto A. Identification of cellular factors binding to acetylated HIV-1 integrase. Amino Acids. 2011;41:1137–45.

    Article  CAS  PubMed  Google Scholar 

  • Allouch A, Di Primio C, Alpi E, Lusic M, Arosio D, Giacca M, Cereseto A. The TRIM family protein KAP1 inhibits HIV-1 integration. Cell Host Microbe. 2011;9:484–95.

    Article  CAS  PubMed  Google Scholar 

  • Berro R, Kehn K, de la Fuente C, Pumfery A, Adair R, Wade J, Colberg-Poley AM, Hiscott J, Kashanchi F. Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32. J Virol. 2006;80:3189–204.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Cereseto A, Manganaro L, Gutierrez MI, Terreni M, Fittipaldi A, Lusic M, Marcello A, Giacca M. Acetylation of HIV-1 integrase by p300 regulates viral integration. Embo J. 2005;24:3070–81.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Chan HM, La Thangue NB. p300/CBP proteins: HATs for transcriptional bridges and scaffolds. J Cell Sci. 2001;114:2363–73.

    CAS  PubMed  Google Scholar 

  • Glozak MA, Sengupta N, Zhang X, Seto E. Acetylation and deacetylation of non-histone proteins. Gene. 2005;363:15–23.

    Article  CAS  PubMed  Google Scholar 

  • Huo L, Li D, Sun L, Liu M, Shi X, Sun X, Li J, Dong B, Dong X, Zhou J. Tat acetylation regulates its actions on microtubule dynamics and apoptosis in T lymphocytes. J Pathol. 2011;223:28–36.

    Article  CAS  PubMed  Google Scholar 

  • Kiernan RE, Vanhulle C, Schiltz L, Adam E, Xiao H, Maudoux F, Calomme C, Burny A, Nakatani Y, Jeang KT, et al. HIV-1 tat transcriptional activity is regulated by acetylation. Embo J. 1999;18:6106–18.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Nakatani Y. HIV-1 transcription: activation mediated by acetylation of Tat. Structure. 2002;10:443–4.

    Article  CAS  PubMed  Google Scholar 

  • Roth SY, Denu JM, Allis CD. Histone acetyltransferases. Annu Rev Biochem. 2001;70:81–120.

    Article  CAS  PubMed  Google Scholar 

  • Schneider WM, Wu DT, Amin V, Aiyer S, Roth MJ. MuLV IN mutants responsive to HDAC inhibitors enhance transcription from unintegrated retroviral DNA. Virology. 2012;426:188–96.

    Article  CAS  PubMed  Google Scholar 

  • Sterner DE, Berger SL. Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev. 2000;64:435–59.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Terreni M, Valentini P, Liverani V, Gutierrez MI, Di Primio C, Di Fenza A, Tozzini V, Allouch A, Albanese A, Giacca M, et al. GCN5-dependent acetylation of HIV-1 integrase enhances viral integration. Retrovirology. 2010;7:18.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  • Wolf D, Goff SP. Embryonic stem cells use ZFP809 to silence retroviral DNAs. Nature. 2009;458:1201–4.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Yang XJ, Seto E. HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention. Oncogene. 2007;26:5310–8.

    Article  CAS  PubMed  Google Scholar 

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Correspondence to Anna Cereseto .

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Cereseto, A. (2018). Acetylation. In: Hope, T.J., Richman, D.D., Stevenson, M. (eds) Encyclopedia of AIDS. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-7101-5_86

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  • DOI: https://doi.org/10.1007/978-1-4939-7101-5_86

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  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4939-7100-8

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