Transglutaminase-induced cross-linking between subdomain 2 of G-actin and the 636-642 lysine-rich loop of myosin subfragment 1

Biophysical Journal
L EligulaA Mühlrád

Abstract

G-actin was covalently cross-linked with S1 in a bacterial transglutaminase-catalyzed reaction. The cross-linking sites were identified with the help of fluorescent probes and limited proteolysis as the Gln-41 on the DNase I binding loop of subdomain 2 in G-actin and a lysine-rich loop (residues 636-642) on the S1 heavy chain. The same lysine-rich loop was cross-linked to another region of G-actin in a former study (Combeau, C., D. Didry, and M-F. Carlier. 1992. J. Biol. Chem. 267:14038-14046). This indicates the existence of more than one G-actin-S1 complex. In contrast to G-actin, no cross-linking was induced between F-actin and S1 by the transglutaminase reaction. This shows that in F-actin the inner part of the DNase I binding loop, where Gln-41 is located, is not accessible for S1. The cross-linked G-actin-S1 polymerized upon addition of 2 mM MgCl2 as indicated by electron microscopy and sedimentation experiments. The filaments obtained from the polymerization of cross-linked actin and S1 were much shorter than the control actin filaments. The ATPase activity of the cross-linked S1 was not activated by actin, whereas the K+ (EDTA)-activated ATPase activity of S1 was unaffected by the cross-linking. The cross-linking betwee...Continue Reading

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Citations

Jul 4, 2008·Amino Acids·Angelo Facchiano, Francesco Facchiano
Jul 27, 2011·Journal of Molecular Neuroscience : MN·Lars DolgeWerner Baumgartner
Dec 12, 2001·Neurochemistry International·Soo Youl KimPeter M Steinert
Oct 9, 2002·Trends in Biochemical Sciences·Laszlo Fesus, Mauro Piacentini
Jan 1, 2013·Plants·Giampiero CaiStefano Del Duca
May 21, 2005·The Journal of Immunology : Official Journal of the American Association of Immunologists·Laura FalascaMauro Piacentini
May 20, 2009·Journal of Agricultural and Food Chemistry·Isain ZapataMacdonald Wick

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