Functional Characterization of the Amino-Terminal Region of Myosin-2
نویسندگان
چکیده
1 Functional Characterization of the Amino-Terminal Region of Myosin-2 Setsuko Fujita-Becker, Georgios Tsiavaliaris, Reiko Ohkura, Takashi Shimada, Dietmar J. Manstein, and Kazuo Sutoh From the Max-Planck-Institut für Medizinische Forschung, Jahnstr. 29, 69120 Heidelberg, Germany; Medizinische Hochschule Hannover, Institut für Biophysikalische Chemie, Carl-Neubergstr.1, 30623 Hannover, Germany, Department of Life Science, University of Tokyo, Komaba 3-8-1, Tokyo 153-8902, Japan.
منابع مشابه
Functional characterization of the N-terminal region of myosin-2.
All class 2 myosins contain an N-terminal extension of approximately 80 residues that includes an Src homology 3 (SH3)-like subdomain. To explore the functional importance of this region, which is also present in most other myosin classes, we generated truncated constructs of Dictyostelium discoideum myosin-2. Truncation at position 80 resulted in the complete loss of myosin-2 function in vivo....
متن کاملSynthesis and Functionalization of Gold Nanoparticles by Using of Poly Functional Amino Acids
Synthesis and characterization of two functionalized gold nanoparticles by using of two poly functional amino acids (L-Arginine and L-Aspartic acid) are reported. The gold nanoparticles were reduced by sodium citrate and functionalized with L-Arginine at the pH of 7 and 11 and L-Aspartic acid at the pH of 7. Transmission electron microscopy, UV-Vis spectroscopy, dynamic light scattering, zeta p...
متن کاملIdentification of functional regions on the tail of Acanthamoeba myosin- II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions
We used purified fusion proteins containing parts of the Acanthamoeba myosin-II tail to localize those regions of the tail responsible for each of the three steps in the successive dimerization mechanism (Sinard, J. H., W. F. Stafford, and T. D. Pollard. 1989. J. Cell Biol. 107:1537-1547) for Acanthamoeba myosin-II minifiliment assembly. Fusion proteins containing the terminal approximately 90%...
متن کاملComparative Kinetic and Functional Characterization of the Motor Domains of Human Nonmuscle Myosin-2C Isoforms*
Nonmuscle myosins are widely distributed and play important roles in the maintenance of cell morphology and cytokinesis. In this study, we compare the detailed kinetic and functional characterization of naturally occurring transcript variants of the motor domain of human nonmuscle myosin heavy chain (NMHC)-2C. NMHC-2C is alternatively spliced both in loop-1 and loop-2. Isoform 2C0 contains no i...
متن کاملTwo Distinct Regions in a Yeast Myosin-V Tail Domain Are Required for the Movement of Different Cargoes
The Saccharomyces cerevisiae myosin-V, Myo2p, is essential for polarized growth, most likely through transport of secretory vesicles to the developing bud. Myo2p is also required for vacuole movement, a process not essential for growth. The globular region of the myosin-V COOH-terminal tail domain is proposed to bind cargo. Through random mutagenesis of this globular tail, we isolated six new s...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2006