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ATPase activity of the microvillar 110 kDa polypeptide‐calmodulin complex is activated in Mg 2+ and inhibited in K + ‐EDTA by F‐actin
Author(s) -
Krizek Janet,
Coluccio Lynne M.,
Bretscher Anthony
Publication year - 1987
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 - 10.1016/0014-5793(87)81172-9
Subject(s) - calmodulin , chemistry , actin , atpase , biochemistry , biophysics , microbiology and biotechnology , biology , enzyme
Highly purified microvillar 110 kDa polypeptide‐calmodulin (110 K‐cam) complex was confirmed to have ATPase activities characteristic of a myosin. The effect of F‐actin on these activities was investigated. The Mg 2+ ‐ATPase is activated about 2‐fold by F‐actin in a dose‐dependent fashion, whereas the K + ‐EDTA ‐ATPase is inhibited by > 90% by F‐actin. These data provide evidence for a functional relationship between the ATPase activity of 110K‐cam and its interaction with F‐actin. They also extend the similarities between 110K‐cam and myosin. The results suggest that higher cells contain in addition to myosin a second class of myosin‐like molecules represented by 110K‐cam.