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A possible regulatory role for the metal‐binding domain of CadA, the Listeria monocytogenes Cd 2+ ‐ATPase
Author(s) -
Bal Nathalie,
Mintz Elisabeth,
Guillain Florent,
Catty Patrice
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02927-1
Subject(s) - atpase , chemistry , phosphorylation , cooperativity , biophysics , biochemistry , microbiology and biotechnology , biology , enzyme
Using the baculovirus/Sf9 expression system, we produced CadA and ΔMBD, a metal‐binding domain, truncated CadA. Both proteins had the expected properties of P‐type ATPases: ATP‐induced Cd 2+ accumulation, Cd 2+ ‐sensitive ATP and Pi phosphorylation and ATPase activity. ΔMBD displayed lower initial transport velocity as well as lower maximal ATPase activity than CadA. MBD truncation flattened the Cd 2+ dependence of the ATPase activity and increased apparent Cd 2+ affinity, suggesting a positive cooperativity between MBD and membranous transport sites. We propose that occupancy of MBD by Cd 2+ modulates CadA activity.