Reversible inhibition of EcoRI with elevated pressure.
The endonuclease activity of EcoRI is completely inhibited at 200 MPa, 37 degrees C using the plasmid pBR 322 as a substrate. When assayed at 133 MPa approximately half the activity at atmospheric pressure was observed; from these data the standard molar volume change is estimated to be -80 cm3mol-1. Upon return to atmospheric pressure the enzyme reacted in a standard manner with its restriction site in pBR 322. Pressurization did not decrease the specificity of the endonuclease activity of the enzyme for its canonical site. These results are discussed in terms of the role of ionic interactions in protein-DNA interactions.
Macgregor
R B
RB
Biophysics Research Department, AT&T Bell Laboratories, Murray Hill, New Jersey 07974.
D001274:Atmospheric Pressure; D004247:DNA / Q000378:metabolism; D015246:Deoxyribonuclease EcoRI / Q000235:genetics / Q000378:metabolism*; D006874:Hydrostatic Pressure; D010957:Plasmids; D011312:Pressure
D004247:DNA; D015246:Deoxyribonuclease EcoRI