Positional effects of monofluorinated phenylalanines on histone acetyltransferase stability and activity.
To explore the impact of global incorporation of fluorinated aromatic amino acids on protein function, we investigated the effects of three monofluorinated phenylalanine analogs para-fluorophenylalanine (pFF), meta-fluorophenylalanine (mFF), and ortho-fluorophenylalanine (oFF) on the stability and enzymatic activity of the histone acetyltransferase (HAT), tGCN5. We selected this set of fluorinated amino acids because they bear the same size and overall polarity but alter in side chain shape and dipole direction. Our experiments showed that among three fluorinated amino acids, the global incorporation of pFF affords the smallest perturbation to the structure and function of tGCN5.
Voloshchuk
Natalya
N
Department of Chemical and Biological Sciences, Polytechnic Institute of New York University, Brooklyn, NY 11201, USA.
Zhu
Anita Y
AY
Snydacker
David
D
Montclare
Jin Kim
JK
D000818:Animals; D004795:Enzyme Stability; D051548:Histone Acetyltransferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry; D011487:Protein Conformation; D015202:Protein Engineering; D016808:Tetrahymena thermophila / Q000201:enzymology*; D010135:p-Fluorophenylalanine / Q000737:chemistry*
C027217:2-fluorophenylalanine; C027218:3-fluorophenylalanine; D010649:Phenylalanine; D010135:p-Fluorophenylalanine; D051548:Histone Acetyltransferases