ADPglucose pyrophosphorylase's N-terminus: structural role in allosteric regulation

Biochemical and Biophysical Research Communications
Clarisa M BejarJ Preiss

Abstract

We studied the functional role of the Escherichia coli ADPglucose pyrophosphorylase's N-terminus in allosteric regulation, and the particular effects caused by its length. Small truncated mutants were designed, and those lacking up to 15-residues were active and highly purified for further kinetic analyses. Ndelta3 and Ndelta7 did not change the kinetic parameters with respect to the wild-type. Ndelta11 and Ndelta15 enzymes were insensitive to allosteric regulation and highly active in the absence of the activator. Co-expression of two polypeptides corresponding to the N- and C-termini generated an enzyme with activation properties lower than those of the wild-type [C.M. Bejar, M.A. Ballicora, D.F. Gómez Casati, A.A. Iglesias, J. Preiss, The ADPglucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains, FEBS Lett. 573 (2004) 99-104]. Here, we characterized a Ndelta15 co-expression mutant, in which the allosteric regulation was restored to wild-type levels. Unusual allosteric effects caused by either an N-terminal truncation or co-expression of individual domains may respond to structural changes favoring an up-regulated or a down-regulated conformation rather than specific activator or inhibito...Continue Reading

References

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Citations

Jul 5, 2013·PloS One·Carlos M FigueroaAlberto A Iglesias
Dec 1, 2015·Frontiers in Microbiology·Ana C EbrechtMiguel A Ballicora
Oct 26, 2016·Protein Science : a Publication of the Protein Society·Eszter NémethBéla Gyurcsik
May 8, 2013·International Journal of Molecular Sciences·Matías D Asención DiezAlberto A Iglesias
Jan 27, 2015·Protein Science : a Publication of the Protein Society·Benjamin L HillMiguel A Ballicora
Nov 3, 2006·The Journal of Biological Chemistry·Clarisa Maria BejarJack Preiss
May 1, 2014·EcoSal Plus·Jack Preiss
Aug 1, 2009·EcoSal Plus·Jack Preiss

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