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Literature summary for 2.3.1.48 extracted from

  • Poveda, A.; Sendra, R.
    Site specificity of yeast histone acetyltransferase B complex in vivo (2008), FEBS J., 275, 2122-2136.
    View publication on PubMed
Search for more literature for 2.3.1.48

Activating Compound

Activating Compound Comment Organism Structure
additional information Hat1 and Hat2, but not Hif1, of the HAT-B complex are required for the Lys12/Lys5-specific acetylation and for histone H4 binding Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
gene hat1, expression of HA-tagged Hat1, HAT-tagged Hat2 and Myc-tagged Hif1 in yeast cells Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information comparison of enzyme activity and cell growth in wild-type and hat1-deficient cells, overview Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Saccharomyces cerevisiae
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + histone H4 Saccharomyces cerevisiae both Lys12 and Lys5 of soluble, non-chromatin-bound histone H4 are in vivo targets of acetylation for the yeast HAT-B enzyme. Lys12/Lys5-acetylated histone H4 is bound to the HAT-B complex in the soluble cell fraction. Exchange of Lys for Arg at position 12 of histone H4 do not interfere with histone H4 association with the complex, but prevented acetylation on Lys5 by the HAT-B enzyme, in vivo as well as in vitro CoA + acetylhistone H4
-
 ?
additional information Saccharomyces cerevisiae soluble histone H4 Hat1-dependently acetylated on Lys12 is present in cells arrested at all cell cycle stages, G1, S, G2/M and also G0. Histone H3 seems to be no substrate for the HAT-B complex ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 wild-type strain W303-1a, gene hat1
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information fairly constant levels of Hat1 protein throughout the cell cycle, soluble histone H4 Hat1-dependently acetylated on Lys12 is present in cells arrested at all cell cycle stages, G1, S, G2/M and also G0 Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + histone H4 both Lys12 and Lys5 of soluble, non-chromatin-bound histone H4 are in vivo targets of acetylation for the yeast HAT-B enzyme. Lys12/Lys5-acetylated histone H4 is bound to the HAT-B complex in the soluble cell fraction. Exchange of Lys for Arg at position 12 of histone H4 do not interfere with histone H4 association with the complex, but prevented acetylation on Lys5 by the HAT-B enzyme, in vivo as well as in vitro Saccharomyces cerevisiae CoA + acetylhistone H4
-
 ?
acetyl-CoA + histone H4 substrates are synthetic N-terminal H4 peptides. The HAT-B complex acetylates only Lys12, recombinant Hat1 is able to modify Lys12 and Lys5. Exchange of Lys for Arg at position 12 of histone H4 does not interfere with histone H4 association with the complex, but prevents acetylation on Lys5 by the HAT-B enzyme, in vivo as well as in vitro Saccharomyces cerevisiae CoA + acetylhistone H4
-
 ?
additional information soluble histone H4 Hat1-dependently acetylated on Lys12 is present in cells arrested at all cell cycle stages, G1, S, G2/M and also G0. Histone H3 seems to be no substrate for the HAT-B complex Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
HAT-B
-
 Saccharomyces cerevisiae
Hat1
-
 Saccharomyces cerevisiae
Hat2
-
 Saccharomyces cerevisiae
histone acetyltransferase B
-
 Saccharomyces cerevisiae
More Hat1, together with Hat2 and Hif1, forms the histone acetyltransferase B, HAT-B, complex Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Saccharomyces cerevisiae