P61A Mutation in the Factor for Inversion Stimulation Results in a Thermostable Dimeric Intermediate†

Biochemistry ◽  
2005 ◽  
Vol 44 (45) ◽  
pp. 14715-14724 ◽  
Author(s):  
Derrick Meinhold ◽  
Sarah Boswell ◽  
Wilfredo Colón
Keyword(s):  
Factor For Inversion Stimulation ◽  
Dimeric Intermediate

Identification of a Dimeric Intermediate in the Unfolding Pathway for the Calcium-Binding Protein S100B

2008 ◽  
Vol 382 (4) ◽  
pp. 1075-1088 ◽  
Author(s):  
Gary S. Shaw ◽  
Nicole M. Marlatt ◽  
Peter L. Ferguson ◽  
Kathryn R. Barber ◽  
Stephen P. Bottomley
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Dimeric Intermediate ◽  
Protein S100b

scholarly journals Comparing the folding landscapes of evolutionarily divergent procaspase-3

2022 ◽  
Author(s):  
Liqi Yao ◽  
Clay Clark
Keyword(s):  
Conformational Change ◽  
Common Ancestor ◽  
Folding Pathway ◽  
Free Energies ◽  
Folding Intermediates ◽  
Effector Caspases ◽  
The Common ◽  
Ph Dependent ◽  
Species Specific ◽  
Dimeric Intermediate

All caspases evolved from a common ancestor and subsequently developed into two general classes, inflammatory or apoptotic caspases. The caspase-hemoglobinase fold has been conserved throughout nearly one billion years of evolution and is utilized for both the monomeric and dimeric subfamilies of apoptotic caspases, called initiator and effector caspases, respectively. We compared the folding and assembly of procaspase-3b from zebrafish to that of human effector procaspases in order to examine the conservation of the folding landscape. Urea-induced equilibrium folding/unfolding of procaspase-3b showed a minimum three-state folding pathway, where the native dimer isomerizes to a partially folded dimeric intermediate, which then unfolds. A partially folded monomeric intermediate observed in the folding landscape of human procaspase-3 is not well-populated in zebrafish procaspase-3b. By comparing effector caspases from different species, we show that the effector procaspase dimer undergoes a pH-dependent conformational change, and that the conformational species in the folding landscape exhibit similar free energies. Together, the data show that the landscape for the caspase-hemoglobinase fold is conserved, yet it provides flexibility for species-specific stabilization or destabilization of folding intermediates resulting in changes in stability. The common pH-dependent conformational change in the native dimer, which yields an enzymatically inactive species, may provide an additional, albeit reversible, mechanism for controlling caspase activity in the cell.

scholarly journals Fis negatively affects binding of Tn4652 transposase by out-competing IHF from the left end of Tn4652

Microbiology ◽  
2009 ◽  
Vol 155 (4) ◽  
pp. 1203-1214 ◽  
Author(s):  
Riho Teras ◽  
Julia Jakovleva ◽  
Maia Kivisaar
Keyword(s):  
Dnase I ◽  
Integration Host Factor ◽  
Mobile Dna ◽  
Mobility Shift ◽  
Transposase Gene ◽  
Transposition Activity ◽  
Global Regulators ◽  
Factor For Inversion Stimulation ◽  
Dna Elements ◽  
Gel Mobility Shift

Transposition activity in bacteria is generally maintained at a low level. The activity of mobile DNA elements can be controlled by bacterially encoded global regulators. Regulation of transposition of Tn4652 in Pseudomonas putida is one such example. Activation of transposition of Tn4652 in starving bacteria requires the stationary-phase sigma factor RpoS and integration host factor (IHF). IHF plays a dual role in Tn4652 translocation by activating transcription of the transposase gene tnpA of the transposon and facilitating TnpA binding to the inverted repeats of the transposon. Our previous results have indicated that besides IHF some other P. putida-encoded global regulator(s) might bind to the ends of Tn4652 and regulate transposition activity. In this study, employing a DNase I footprint assay we have identified a binding site of P. putida Fis (factor for inversion stimulation) centred 135 bp inside the left end of Tn4652. Our results of gel mobility shift and DNase I footprint studies revealed that Fis out-competes IHF from the left end of Tn4652, thereby abolishing the binding of TnpA. Thus, the results obtained in this study indicate that the transposition of Tn4652 is regulated by the cellular amount of P. putida global regulators Fis and IHF.

Evidence of a Thermal Unfolding Dimeric Intermediate for the Escherichia coli Histone-like HU Proteins: Thermodynamics and Structure

2003 ◽  
Vol 331 (1) ◽  
pp. 101-121 ◽  
Author(s):  
Jean Ramstein ◽  
Nadège Hervouet ◽  
Franck Coste ◽  
Charles Zelwer ◽  
Jacques Oberto ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Thermal Unfolding ◽  
Hu Proteins ◽  
Dimeric Intermediate

Biosynthesis of the lupine alkaloids. I. Lupinine

1985 ◽  
Vol 63 (10) ◽  
pp. 2707-2718 ◽  
Author(s):  
W. Marek Golebiewski ◽  
Ian D. Spenser
Keyword(s):  
Nmr Spectroscopy ◽  
H Nmr ◽  
Dimeric Intermediate ◽  
C Nmr

The mode of incorporation into lupinine of cadaverine, intramolecularly doubly labelled with,15N and with,13C at the C-atom adjacent to 15N, i.e., 13C, 15N-"bond-labelled", was determined by,13C nmr spectroscopy; lupinine is generated from two cadaverine-derived C5-units by a route which excludes a "dimeric" intermediate with C2v symmetry. The mode of incorporation of 2H from L-(2-2H)lysine, from (R)- and (S)-(1-2H)cadaverine, and from (2-2H)-Δ1-piperideine into lupinine was determined by 2H nmr spectroscopy. The results corroborate the conclusions from the 13C,15N experiment and they establish the stereochemistry of six of the steps in the biosynthetic conversion of L-lysine into lupinine.

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