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Sharing the SAGA.

Helmlinger D, Tora L.

Trends Biochem Sci. 2017 Nov;42(11):850-861. doi: 10.1016/j.tibs.2017.09.001. Epub 2017 Sep 27. Review.


Elimination of truncated recombinant protein expressed in Escherichia coli by removing cryptic translation initiation site.

Jennings MJ, Barrios AF, Tan S.

Protein Expr Purif. 2016 May;121:17-21. doi: 10.1016/j.pep.2015.12.001. Epub 2015 Dec 29.


SWI/SNF recruitment to a DNA double-strand break by the NuA4 and Gcn5 histone acetyltransferases.

Bennett G, Peterson CL.

DNA Repair (Amst). 2015 Jun;30:38-45. doi: 10.1016/j.dnarep.2015.03.006. Epub 2015 Mar 25.


Distinct roles of the Gcn5 histone acetyltransferase revealed during transient stress-induced reprogramming of the genome.

Xue-Franzén Y, Henriksson J, Bürglin TR, Wright AP.

BMC Genomics. 2013 Jul 16;14:479. doi: 10.1186/1471-2164-14-479.


Genome-wide characterisation of the Gcn5 histone acetyltransferase in budding yeast during stress adaptation reveals evolutionarily conserved and diverged roles.

Xue-Franzén Y, Johnsson A, Brodin D, Henriksson J, Bürglin TR, Wright AP.

BMC Genomics. 2010 Mar 25;11:200. doi: 10.1186/1471-2164-11-200.


Gcn5 promotes acetylation, eviction, and methylation of nucleosomes in transcribed coding regions.

Govind CK, Zhang F, Qiu H, Hofmeyer K, Hinnebusch AG.

Mol Cell. 2007 Jan 12;25(1):31-42.


Stress-specific role of fission yeast Gcn5 histone acetyltransferase in programming a subset of stress response genes.

Johnsson A, Xue-Franzén Y, Lundin M, Wright AP.

Eukaryot Cell. 2006 Aug;5(8):1337-46.


A role for gcn5-mediated global histone acetylation in transcriptional regulation.

Imoberdorf RM, Topalidou I, Strubin M.

Mol Cell Biol. 2006 Mar;26(5):1610-6.


Sumoylation of the yeast Gcn5 protein.

Sterner DE, Nathan D, Reindle A, Johnson ES, Berger SL.

Biochemistry. 2006 Jan 24;45(3):1035-42.


The role of loop ZA and Pro371 in the function of yeast Gcn5p bromodomain revealed through molecular dynamics and experiment.

Pizzitutti F, Giansanti A, Ballario P, Ornaghi P, Torreri P, Ciccotti G, Filetici P.

J Mol Recognit. 2006 Jan-Feb;19(1):1-9.


Hyperacetylation of chromatin at the ADH2 promoter allows Adr1 to bind in repressed conditions.

Verdone L, Wu J, van Riper K, Kacherovsky N, Vogelauer M, Young ET, Grunstein M, Di Mauro E, Caserta M.

EMBO J. 2002 Mar 1;21(5):1101-11.


Gcn5p is involved in the acetylation of histone H3 in nucleosomes.

Ruiz-García AB, Sendra R, Pamblanco M, Tordera V.

FEBS Lett. 1997 Feb 17;403(2):186-90.


Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation.

Brownell JE, Zhou J, Ranalli T, Kobayashi R, Edmondson DG, Roth SY, Allis CD.

Cell. 1996 Mar 22;84(6):843-51.


Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2.

Sun J, Paduch M, Kim SA, Kramer RM, Barrios AF, Lu V, Luke J, Usatyuk S, Kossiakoff AA, Tan S.

Proc Natl Acad Sci U S A. 2018 Oct 2;115(40):10010-10015. doi: 10.1073/pnas.1805343115. Epub 2018 Sep 17.


Distinct patterns of histone acetyltransferase and Mediator deployment at yeast protein-coding genes.

Bruzzone MJ, Grünberg S, Kubik S, Zentner GE, Shore D.

Genes Dev. 2018 Sep 1;32(17-18):1252-1265. doi: 10.1101/gad.312173.118. Epub 2018 Aug 14.


SAGA complex and Gcn5 are necessary for respiration in budding yeast.

Canzonetta C, Leo M, Guarino SR, Montanari A, Francisci S, Filetici P.

Biochim Biophys Acta. 2016 Dec;1863(12):3160-3168. doi: 10.1016/j.bbamcr.2016.10.002. Epub 2016 Oct 11.


Chromatin dynamics during DNA replication.

Bar-Ziv R, Voichek Y, Barkai N.

Genome Res. 2016 Sep;26(9):1245-56. doi: 10.1101/gr.201244.115. Epub 2016 May 25.


Wine yeast sirtuins and Gcn5p control aging and metabolism in a natural growth medium.

Orozco H, Matallana E, Aranda A.

Mech Ageing Dev. 2012 May;133(5):348-58. doi: 10.1016/j.mad.2012.03.013. Epub 2012 Apr 2.


Gcn5 regulates the dissociation of SWI/SNF from chromatin by acetylation of Swi2/Snf2.

Kim JH, Saraf A, Florens L, Washburn M, Workman JL.

Genes Dev. 2010 Dec 15;24(24):2766-71. doi: 10.1101/gad.1979710.

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