A1 Refereed original research article in a scientific journal

Cd2+-induced aggregation of Escherichia coli pyrophosphatase




AuthorsZimenkov YV, Salminen A, Efimova IS, Lahti R, Baykov AA

PublisherBLACKWELL PUBLISHING LTD

Publication year2004

JournalEuropean Journal of Biochemistry

Journal name in sourceEUROPEAN JOURNAL OF BIOCHEMISTRY

Journal acronymEUR J BIOCHEM

Volume271

Issue14

First page 3064

Last page3067

Number of pages4

ISSN0014-2956

DOIhttps://doi.org/10.1111/j.1432-1033.2004.04239.x(external)


Abstract
We report here that Escherichia coli pyrophosphatase aggregates in the presence of millimolar Cd2+. This highly cooperative process was specific to both the metal ion and the protein and could be reversed fully by decreasing the Cd2+ concentration. Aggregation was enhanced by Mg2+, the natural cofactor of pyrophosphatase, and Mn2+. Mutations at the intersubunit metal-binding site had no effect, whereas mutation at Glu139, which is part of the peripheral metal-binding site found in pyrophosphatase crystals near the contact region between two enzyme molecules, suppressed aggregation. These findings indicate that aggregation is affected by Cd2+ binding to the peripheral metal-binding site, probably by strengthening intermolecular Trp149-Trp149' stacking interactions.



Last updated on 2024-26-11 at 14:57