PMID- 2140947
OWN - NLM
STAT- MEDLINE
DCOM- 19900716
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 29
IP  - 18
DP  - 1990 May 8
TI  - Activation of Escherichia coli F1-ATPase by lauryldimethylamine oxide and 
      ethylene glycol: relationship of ATPase activity to the interaction of the 
      epsilon and beta subunits.
PG  - 4335-40
AB  - The stimulation of the ATPase activity of Escherichia coli F1-ATPase by the 
      detergent lauryldimethylamine oxide (LDAO) and the relationship of this 
      activation to removal of the inhibitory epsilon subunit were studied. The 
      detergent caused a dramatic decrease in the affinity of epsilon-depleted enzyme 
      for epsilon subunit, suggesting that release of epsilon is involved in LDAO 
      activation. However, even in the absence of any epsilon subunit, the detergent 
      caused a 140% increase in activity, indicating activation by effects independent 
      of epsilon. In contrast, the addition of 30% ethylene glycol to the reaction 
      buffer caused a modest inhibition of the ATPase activity of epsilon-depleted 
      F1-ATPase but rendered the enzyme insensitive to inhibition by epsilon subunit. 
      This solvent prevented the cross-linking of epsilon to beta by a water-soluble 
      carbodiimide, although epsilon remained linkable to both beta and gamma by 
      dithiobis(succinimidyl propionate). Thus, epsilon was not dissociated from 
      F1-ATPase, but its intimate interaction with the beta subunit was altered. These 
      results suggest that the inhibitory action of epsilon is expressed through its 
      interaction with beta. Kinetic analysis revealed that LDAO activated hydrolysis 
      at both the high- and low-affinity promotional sites, with little change in Km 
      values. Ethylene glycol caused a substantial increase in Km at the low-affinity 
      promotional site and made the enzyme resistant to inhibition by aurovertin D.
FAU - Dunn, S D
AU  - Dunn SD
AD  - Department of Biochemistry, University of Western Ontario, London, Canada.
FAU - Tozer, R G
AU  - Tozer RG
FAU - Zadorozny, V D
AU  - Zadorozny VD
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Cross-Linking Reagents)
RN  - 0 (Detergents)
RN  - 0 (Dimethylamines)
RN  - 0 (Ethylene Glycols)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Surface-Active Agents)
RN  - 4F6FC4MI8W (dodecyldimethylamine oxide)
RN  - EC 3.6.3.14 (Proton-Translocating ATPases)
RN  - FC72KVT52F (Ethylene Glycol)
SB  - IM
MH  - Cross-Linking Reagents
MH  - Detergents/*pharmacology
MH  - Dimethylamines/*pharmacology
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme Activation
MH  - Escherichia coli/*enzymology
MH  - Ethylene Glycol
MH  - Ethylene Glycols/*pharmacology
MH  - Kinetics
MH  - Macromolecular Substances
MH  - Molecular Weight
MH  - Proton-Translocating ATPases/*metabolism
MH  - Surface-Active Agents/*pharmacology
EDAT- 1990/05/08 00:00
MHDA- 1990/05/08 00:01
CRDT- 1990/05/08 00:00
PHST- 1990/05/08 00:00 [pubmed]
PHST- 1990/05/08 00:01 [medline]
PHST- 1990/05/08 00:00 [entrez]
AID - 10.1021/bi00470a011 [doi]
PST - ppublish
SO  - Biochemistry. 1990 May 8;29(18):4335-40. doi: 10.1021/bi00470a011.