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Structural and Functional Role of Acetyltransferase hMOF K274 Autoacetylation.

J. Biol. Chem.. 2016; 
McCullough Cheryl E,Song Shufei,Shin Michael H,Johnson F Brad,Marmorstein R
Products/Services Used Details Operation
Peptide Synthesis Briefly, 50 nM hMOF or 200 nM MOZ was incubated with 400 ␮M substrate peptide (H4(1–19) peptide for hMOF and H3(1–19) for MOZ) (GenScript) and 50 ␮M [14C]acetyl-CoA (50 – 60 mCi/mmol, Moravek) in reaction buffer (100 mM ace- tate, 50 mM Bistris, 50 mM Tris at various pH values 100 mM NaCl, 800 ␮M cysteine, and 0. Get A Quote

摘要

Many histone acetyltransferases undergo autoacetylation, either through chemical or enzymatic means, to potentiate enzymatic cognate substrate lysine acetylation, although the mode and molecular role of such autoacetylation is poorly understood. The MYST family of histone acetyltransferases is autoacetylated at an active site lysine residue to facilitate cognate substrate lysine binding and acetylation. Here, we report on a detailed molecular investigation of Lys-274 autoacetylation of the human MYST protein Males Absent on the First (hMOF). A mutational scan of hMOF Lys-274 reveals that all amino acid substitutions of this residue are able to bind cofactor but are significantly destabilized, both in ... More

关键词

acetyl coenzyme A (acetyl-CoA),acetylation,chemical modification,histone acetylase,post-translational modification (