Sandbox Reserved 774: Difference between revisions

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=Histone Acetyltransferase Hpa2=
=Histone Acetyltransferase Hpa2=


Hpa2 is a member of the GNAT (Gcn5-related N-acetyltransferases) super-family of enzymes that are found spread out across nature and use acyl-CoA's to acylate their cognate substrates.<ref name=desperate>"Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae." Protein Data Bank. EMDataBank, n.d. Web. 17 Nov. 2013.[http://www.rcsb.org/pdb/explore/explore.do?structureId=1QSO RCSB.org]</ref> Histone Acetyltransferase Hpa2 is found in the organism Saccharomyces Cerevisiae, which is more commonly known as Baker's Yeast.<ref>"Q06592 (HPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot." Unitprot.org. UniProtKB, 13 Nov. 2013. Web. 16 Nov. 2013.[http://www.uniprot.org/uniprot/Q06592 UnitPro.org]</ref> It was also discovered in other organisms, such as Pelagibacterium halotolerans B2 - a marine halotolerant bacterium in the East China Sea. <ref>Huo. "Complete Genome Sequence of Pelagibacterium Halotolerans B2(T)." J. Bacteriol 197.8 (2012): 1. Web. 26 Nov. 2013. [http://www.ncbi.nlm.nih.gov/pubmed/22156395 NCBI.nlm.nih.gov]</ref> In vitro, Hpa2 serves to acetylate histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12.' In solution, Hpa2 forms a dimer, and upon binding with AcCoA forms a tetramer.<ref name=desperate/><ref name=Shiva/> It is classified as a transferase.<ref name=Shiva>Angus-Hill, et al. "Crystal Structure of the Histone Acetyltransferase Hpa2: a Tetrameric Member of the Gcn5-related N-acetyltransferase Superfamily." J. Mol. Biol. 1999.3338 (1999): 1-14. Web. 18 Nov. 2013.</ref>
Histone Acetyltransferase Hpa2 is a member of the GNAT (Gcn5-related N-acetyltransferases) super-family of enzymes that are found spread out across nature and use acyl-CoA's to acylate their cognate substrates.<ref name=desperate>"Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae." Protein Data Bank. EMDataBank, n.d. Web. 17 Nov. 2013.[http://www.rcsb.org/pdb/explore/explore.do?structureId=1QSO RCSB.org]</ref> GNAT is a catalytic subunit of ADA and SAGA histone acetyltransferase complexes. <ref>"GCN5/YGR252W Summary." YeastGenome.org. Standford University, n.d. Web. 26 Nov. 2013. [http://www.yeastgenome.org/cgi-bin/locus.fpl?locus=gcn5 YeastGenome.org]</ref>Hpa2 is found in the organism Saccharomyces Cerevisiae, which is more commonly known as Baker's Yeast.<ref>"Q06592 (HPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot." Unitprot.org. UniProtKB, 13 Nov. 2013. Web. 16 Nov. 2013.[http://www.uniprot.org/uniprot/Q06592 UnitPro.org]</ref> It was also discovered in other organisms, such as Pelagibacterium halotolerans B2 - a marine halotolerant bacterium in the East China Sea. <ref>Huo. "Complete Genome Sequence of Pelagibacterium Halotolerans B2(T)." J. Bacteriol 197.8 (2012): 1. Web. 26 Nov. 2013. [http://www.ncbi.nlm.nih.gov/pubmed/22156395 NCBI.nlm.nih.gov]</ref> In vitro, Hpa2 serves to acetylate histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12.' In solution, Hpa2 forms a dimer, and upon binding with AcCoA forms a tetramer.<ref name=desperate/><ref name=Shiva/> It is classified as a transferase.<ref name=Shiva>Angus-Hill, et al. "Crystal Structure of the Histone Acetyltransferase Hpa2: a Tetrameric Member of the Gcn5-related N-acetyltransferase Superfamily." J. Mol. Biol. 1999.3338 (1999): 1-14. Web. 18 Nov. 2013.</ref>


=Structure=
=Structure=
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